CA1307736C - Methode de dosage immunologique de l'inhibine - Google Patents

Methode de dosage immunologique de l'inhibine

Info

Publication number: CA1307736C
Authority: CA; Canada
Prior art keywords: inhibin; radioimmunoassay; serum; sample; bovine
Prior art date: 1986-03-13
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Lifetime

Application number

CA000531961A

Other languages

English (en)

Inventor

David Mark Robertson

Robert Ian Mclachlan

David Moritz De Kretser

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Monash Medical Centre

St Vincents Institute of Medical Research

Inhibin Pty Ltd

Monash University

Original Assignee

Monash Medical Centre

St Vincents Institute of Medical Research

Monash University

Biotechnology Australia Pty Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1986-03-13

Filing date

1987-03-13

Publication date

1992-09-22

1987-03-13 Application filed by Monash Medical Centre, St Vincents Institute of Medical Research, Monash University, Biotechnology Australia Pty Ltd filed Critical Monash Medical Centre

1992-09-22 Application granted granted Critical

1992-09-22 Publication of CA1307736C publication Critical patent/CA1307736C/fr

2009-09-22 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

Links

239000000893 inhibin Substances 0.000 title claims abstract description 264
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 title claims abstract description 258
238000003556 assay Methods 0.000 title claims abstract description 50
238000000034 method Methods 0.000 title claims abstract description 29
238000003127 radioimmunoassay Methods 0.000 claims abstract description 37
239000012634 fragment Substances 0.000 claims abstract description 7
241001465754 Metazoa Species 0.000 claims abstract description 5
108010001267 Protein Subunits Chemical group 0.000 claims abstract description 5
239000000427 antigen Substances 0.000 claims abstract description 4
108091007433 antigens Proteins 0.000 claims abstract description 4
102000036639 antigens Human genes 0.000 claims abstract description 4
210000002966 serum Anatomy 0.000 claims description 67
241000283690 Bos taurus Species 0.000 claims description 39
239000000523 sample Substances 0.000 claims description 20
238000000338 in vitro Methods 0.000 claims description 19
238000011534 incubation Methods 0.000 claims description 14
230000002611 ovarian Effects 0.000 claims description 13
230000016087 ovulation Effects 0.000 claims description 13
210000000287 oocyte Anatomy 0.000 claims description 12
210000002503 granulosa cell Anatomy 0.000 claims description 11
239000000463 material Substances 0.000 claims description 10
230000035935 pregnancy Effects 0.000 claims description 8
241000124008 Mammalia Species 0.000 claims description 7
VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 claims description 6
230000006698 induction Effects 0.000 claims description 6
238000012360 testing method Methods 0.000 claims description 6
230000008217 follicular development Effects 0.000 claims description 5
210000002394 ovarian follicle Anatomy 0.000 claims description 5
230000003915 cell function Effects 0.000 claims description 4
230000004720 fertilization Effects 0.000 claims description 4
238000002523 gelfiltration Methods 0.000 claims description 4
206010033266 Ovarian Hyperstimulation Syndrome Diseases 0.000 claims description 3
239000002202 Polyethylene glycol Substances 0.000 claims description 3
229920004890 Triton X-100 Polymers 0.000 claims description 3
239000013504 Triton X-100 Substances 0.000 claims description 3
239000012472 biological sample Substances 0.000 claims description 3
230000036541 health Effects 0.000 claims description 3
210000004681 ovum Anatomy 0.000 claims description 3
229920001223 polyethylene glycol Polymers 0.000 claims description 3
239000002244 precipitate Substances 0.000 claims description 3
108020004511 Recombinant DNA Proteins 0.000 claims description 2
238000005516 engineering process Methods 0.000 claims description 2
230000006870 function Effects 0.000 claims description 2
230000035800 maturation Effects 0.000 claims description 2
230000001850 reproductive effect Effects 0.000 claims description 2
210000000717 sertoli cell Anatomy 0.000 claims description 2
230000036642 wellbeing Effects 0.000 claims description 2
102000002067 Protein Subunits Human genes 0.000 claims 1
238000001042 affinity chromatography Methods 0.000 claims 1
230000002083 iodinating effect Effects 0.000 claims 1
238000012544 monitoring process Methods 0.000 claims 1
229960001479 tosylchloramide sodium Drugs 0.000 claims 1
239000000700 radioactive tracer Substances 0.000 abstract description 31
238000003018 immunoassay Methods 0.000 abstract description 6
238000002965 ELISA Methods 0.000 abstract description 2
108010004250 Inhibins Proteins 0.000 description 224
102000002746 Inhibins Human genes 0.000 description 224
210000002381 plasma Anatomy 0.000 description 39
238000002360 preparation method Methods 0.000 description 24
RJKFOVLPORLFTN-LEKSSAKUSA-N Progesterone Chemical compound C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](C(=O)C)[C@@]1(C)CC2 RJKFOVLPORLFTN-LEKSSAKUSA-N 0.000 description 18
210000001733 follicular fluid Anatomy 0.000 description 18
VOXZDWNPVJITMN-ZBRFXRBCSA-N 17β-estradiol Chemical compound OC1=CC=C2[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 VOXZDWNPVJITMN-ZBRFXRBCSA-N 0.000 description 16
230000000694 effects Effects 0.000 description 16
229930182833 estradiol Natural products 0.000 description 16
230000035945 sensitivity Effects 0.000 description 13
241000473945 Theria <moth genus> Species 0.000 description 12
229940088597 hormone Drugs 0.000 description 12
239000005556 hormone Substances 0.000 description 12
230000026045 iodination Effects 0.000 description 12
238000006192 iodination reaction Methods 0.000 description 12
241000700159 Rattus Species 0.000 description 10
230000027455 binding Effects 0.000 description 10
238000004166 bioassay Methods 0.000 description 10
239000008363 phosphate buffer Substances 0.000 description 10
238000000746 purification Methods 0.000 description 10
231100000673 dose–response relationship Toxicity 0.000 description 9
230000029849 luteinization Effects 0.000 description 9
239000000186 progesterone Substances 0.000 description 9
229960003387 progesterone Drugs 0.000 description 9
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 9
241000283973 Oryctolagus cuniculus Species 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
238000006386 neutralization reaction Methods 0.000 description 7
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
229920005654 Sephadex Polymers 0.000 description 6
239000012507 Sephadex™ Substances 0.000 description 6
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 6
239000000872 buffer Substances 0.000 description 6
210000004027 cell Anatomy 0.000 description 6
239000003610 charcoal Substances 0.000 description 6
238000006073 displacement reaction Methods 0.000 description 6
238000005194 fractionation Methods 0.000 description 6
JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 6
230000003472 neutralizing effect Effects 0.000 description 6
241000894007 species Species 0.000 description 6
PYTMYKVIJXPNBD-OQKDUQJOSA-N 2-[4-[(z)-2-chloro-1,2-diphenylethenyl]phenoxy]-n,n-diethylethanamine;hydron;2-hydroxypropane-1,2,3-tricarboxylate Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O.C1=CC(OCCN(CC)CC)=CC=C1C(\C=1C=CC=CC=1)=C(/Cl)C1=CC=CC=C1 PYTMYKVIJXPNBD-OQKDUQJOSA-N 0.000 description 5
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 5
239000000499 gel Substances 0.000 description 5
235000019333 sodium laurylsulphate Nutrition 0.000 description 5
238000003744 In vitro fertilisation Methods 0.000 description 4
239000012506 Sephacryl® Substances 0.000 description 4
239000012131 assay buffer Substances 0.000 description 4
230000004071 biological effect Effects 0.000 description 4
210000004369 blood Anatomy 0.000 description 4
239000008280 blood Substances 0.000 description 4
244000309464 bull Species 0.000 description 4
230000009260 cross reactivity Effects 0.000 description 4
238000010790 dilution Methods 0.000 description 4
239000012895 dilution Substances 0.000 description 4
239000000284 extract Substances 0.000 description 4
230000027758 ovulation cycle Effects 0.000 description 4
230000009467 reduction Effects 0.000 description 4
230000004044 response Effects 0.000 description 4
238000004007 reversed phase HPLC Methods 0.000 description 4
239000011780 sodium chloride Substances 0.000 description 4
239000011800 void material Substances 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
102000003846 Carbonic anhydrases Human genes 0.000 description 3
108090000209 Carbonic anhydrases Proteins 0.000 description 3
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
102000003886 Glycoproteins Human genes 0.000 description 3
108090000288 Glycoproteins Proteins 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
239000012888 bovine serum Substances 0.000 description 3
238000004364 calculation method Methods 0.000 description 3
239000004202 carbamide Substances 0.000 description 3
238000004113 cell culture Methods 0.000 description 3
229940046989 clomiphene citrate Drugs 0.000 description 3
230000000875 corresponding effect Effects 0.000 description 3
230000037029 cross reaction Effects 0.000 description 3
239000012530 fluid Substances 0.000 description 3
230000001900 immune effect Effects 0.000 description 3
238000001727 in vivo Methods 0.000 description 3
239000003550 marker Substances 0.000 description 3
238000005259 measurement Methods 0.000 description 3
239000002609 medium Substances 0.000 description 3
108090000765 processed proteins & peptides Proteins 0.000 description 3
102000004169 proteins and genes Human genes 0.000 description 3
108090000623 proteins and genes Proteins 0.000 description 3
238000011084 recovery Methods 0.000 description 3
230000002829 reductive effect Effects 0.000 description 3
210000002830 rete testis Anatomy 0.000 description 3
210000001550 testis Anatomy 0.000 description 3
210000001519 tissue Anatomy 0.000 description 3
239000002023 wood Substances 0.000 description 3
CBUWTGCATVNMJE-UHFFFAOYSA-N 6,6-dimethylheptanal Chemical compound CC(C)(C)CCCCC=O CBUWTGCATVNMJE-UHFFFAOYSA-N 0.000 description 2
108010005853 Anti-Mullerian Hormone Proteins 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
241000283707 Capra Species 0.000 description 2
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
102000011022 Chorionic Gonadotropin Human genes 0.000 description 2
108010062540 Chorionic Gonadotropin Proteins 0.000 description 2
108010057021 Menotropins Proteins 0.000 description 2
108010058846 Ovalbumin Proteins 0.000 description 2
229910019142 PO4 Inorganic materials 0.000 description 2
208000002500 Primary Ovarian Insufficiency Diseases 0.000 description 2
230000029936 alkylation Effects 0.000 description 2
238000005804 alkylation reaction Methods 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
239000000868 anti-mullerian hormone Substances 0.000 description 2
230000033228 biological regulation Effects 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
239000006143 cell culture medium Substances 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
230000002596 correlated effect Effects 0.000 description 2
210000000172 cytosol Anatomy 0.000 description 2
238000001514 detection method Methods 0.000 description 2
239000012502 diagnostic product Substances 0.000 description 2
239000000539 dimer Substances 0.000 description 2
238000010494 dissociation reaction Methods 0.000 description 2
230000005593 dissociations Effects 0.000 description 2
238000001641 gel filtration chromatography Methods 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
239000001963 growth medium Substances 0.000 description 2
238000004128 high performance liquid chromatography Methods 0.000 description 2
229940090343 human menopausal gonadotrophin Drugs 0.000 description 2
238000002649 immunization Methods 0.000 description 2
230000003053 immunization Effects 0.000 description 2
230000005764 inhibitory process Effects 0.000 description 2
150000002500 ions Chemical class 0.000 description 2
238000002357 laparoscopic surgery Methods 0.000 description 2
210000002751 lymph Anatomy 0.000 description 2
210000001161 mammalian embryo Anatomy 0.000 description 2
230000002175 menstrual effect Effects 0.000 description 2
230000009871 nonspecific binding Effects 0.000 description 2
229940092253 ovalbumin Drugs 0.000 description 2
210000001672 ovary Anatomy 0.000 description 2
238000007427 paired t-test Methods 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
230000001817 pituitary effect Effects 0.000 description 2
229940064298 pregnyl Drugs 0.000 description 2
206010036601 premature menopause Diseases 0.000 description 2
208000017942 premature ovarian failure 1 Diseases 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
239000002904 solvent Substances 0.000 description 2
239000000126 substance Substances 0.000 description 2
238000012546 transfer Methods 0.000 description 2
230000009466 transformation Effects 0.000 description 2
238000002604 ultrasonography Methods 0.000 description 2
KYRUKRFVOACELK-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(4-hydroxyphenyl)propanoate Chemical compound C1=CC(O)=CC=C1CCC(=O)ON1C(=O)CCC1=O KYRUKRFVOACELK-UHFFFAOYSA-N 0.000 description 1
FJQZXCPWAGYPSD-UHFFFAOYSA-N 1,3,4,6-tetrachloro-3a,6a-diphenylimidazo[4,5-d]imidazole-2,5-dione Chemical compound ClN1C(=O)N(Cl)C2(C=3C=CC=CC=3)N(Cl)C(=O)N(Cl)C12C1=CC=CC=C1 FJQZXCPWAGYPSD-UHFFFAOYSA-N 0.000 description 1
PENWAFASUFITRC-UHFFFAOYSA-N 2-(4-chlorophenyl)imidazo[2,1-a]isoquinoline Chemical compound C1=CC(Cl)=CC=C1C1=CN(C=CC=2C3=CC=CC=2)C3=N1 PENWAFASUFITRC-UHFFFAOYSA-N 0.000 description 1
ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
241000272814 Anser sp. Species 0.000 description 1
208000002109 Argyria Diseases 0.000 description 1
241000271566 Aves Species 0.000 description 1
101710125089 Bindin Proteins 0.000 description 1
241000282472 Canis lupus familiaris Species 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 1
201000009273 Endometriosis Diseases 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
241000283086 Equidae Species 0.000 description 1
241000283074 Equus asinus Species 0.000 description 1
-1 FS~ Chemical compound 0.000 description 1
241000287828 Gallus gallus Species 0.000 description 1
HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
241000282412 Homo Species 0.000 description 1
101000904173 Homo sapiens Progonadoliberin-1 Proteins 0.000 description 1
101000637771 Homo sapiens Solute carrier family 35 member G1 Proteins 0.000 description 1
DOMWKUIIPQCAJU-LJHIYBGHSA-N Hydroxyprogesterone caproate Chemical compound C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@@](C(C)=O)(OC(=O)CCCCC)[C@@]1(C)CC2 DOMWKUIIPQCAJU-LJHIYBGHSA-N 0.000 description 1
108010023244 Lactoperoxidase Proteins 0.000 description 1
102000045576 Lactoperoxidases Human genes 0.000 description 1
229920006063 Lamide® Polymers 0.000 description 1
WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
241000699670 Mus sp. Species 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
RQTDRJMAUKHGHV-UHFFFAOYSA-N P.P.I Chemical compound P.P.I RQTDRJMAUKHGHV-UHFFFAOYSA-N 0.000 description 1
241001494479 Pecora Species 0.000 description 1
208000037062 Polyps Diseases 0.000 description 1
102100024028 Progonadoliberin-1 Human genes 0.000 description 1
101000996723 Sus scrofa Gonadotropin-releasing hormone receptor Proteins 0.000 description 1
108090001012 Transforming Growth Factor beta Proteins 0.000 description 1
102000004887 Transforming Growth Factor beta Human genes 0.000 description 1
208000026928 Turner syndrome Diseases 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
230000000890 antigenic effect Effects 0.000 description 1
230000000975 bioactive effect Effects 0.000 description 1
239000013060 biological fluid Substances 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
238000009835 boiling Methods 0.000 description 1
UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
235000013330 chicken meat Nutrition 0.000 description 1
229960004407 chorionic gonadotrophin Drugs 0.000 description 1
238000011210 chromatographic step Methods 0.000 description 1
238000010367 cloning Methods 0.000 description 1
230000009137 competitive binding Effects 0.000 description 1
239000002299 complementary DNA Substances 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
239000012531 culture fluid Substances 0.000 description 1
230000007423 decrease Effects 0.000 description 1
230000003111 delayed effect Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000013461 design Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
239000003085 diluting agent Substances 0.000 description 1
150000002009 diols Chemical class 0.000 description 1
201000010099 disease Diseases 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
238000009826 distribution Methods 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
229940088598 enzyme Drugs 0.000 description 1
229960005309 estradiol Drugs 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
238000009093 first-line therapy Methods 0.000 description 1
238000001917 fluorescence detection Methods 0.000 description 1
230000003325 follicular Effects 0.000 description 1
239000004459 forage Substances 0.000 description 1
238000007710 freezing Methods 0.000 description 1
230000008014 freezing Effects 0.000 description 1
238000001502 gel electrophoresis Methods 0.000 description 1
238000005227 gel permeation chromatography Methods 0.000 description 1
XLXSAKCOAKORKW-UHFFFAOYSA-N gonadorelin Chemical compound C1CCC(C(=O)NCC(N)=O)N1C(=O)C(CCCN=C(N)N)NC(=O)C(CC(C)C)NC(=O)CNC(=O)C(NC(=O)C(CO)NC(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C(CC=1NC=NC=1)NC(=O)C1NC(=O)CC1)CC1=CC=C(O)C=C1 XLXSAKCOAKORKW-UHFFFAOYSA-N 0.000 description 1
210000004368 gonadotroph Anatomy 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
229960002897 heparin Drugs 0.000 description 1
229920000669 heparin Polymers 0.000 description 1
102000053339 human SLC35G1 Human genes 0.000 description 1
230000028993 immune response Effects 0.000 description 1
239000003547 immunosorbent Substances 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
208000000509 infertility Diseases 0.000 description 1
230000036512 infertility Effects 0.000 description 1
231100000535 infertility Toxicity 0.000 description 1
208000021267 infertility disease Diseases 0.000 description 1
238000002347 injection Methods 0.000 description 1
239000007924 injection Substances 0.000 description 1
238000007918 intramuscular administration Methods 0.000 description 1
229910052740 iodine Inorganic materials 0.000 description 1
239000011630 iodine Substances 0.000 description 1
229940057428 lactoperoxidase Drugs 0.000 description 1
108010052322 limitin Proteins 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
229910052744 lithium Inorganic materials 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
238000004519 manufacturing process Methods 0.000 description 1
108020004999 messenger RNA Proteins 0.000 description 1
239000000203 mixture Substances 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
238000011587 new zealand white rabbit Methods 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
230000011599 ovarian follicle development Effects 0.000 description 1
230000000624 ovulatory effect Effects 0.000 description 1
230000002688 persistence Effects 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
230000000063 preceeding effect Effects 0.000 description 1
230000001376 precipitating effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
239000000047 product Substances 0.000 description 1
230000000750 progressive effect Effects 0.000 description 1
238000011002 quantification Methods 0.000 description 1
230000002285 radioactive effect Effects 0.000 description 1
239000011541 reaction mixture Substances 0.000 description 1
230000009257 reactivity Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
238000013391 scatchard analysis Methods 0.000 description 1
HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 description 1
239000004296 sodium metabisulphite Substances 0.000 description 1
235000010262 sodium metabisulphite Nutrition 0.000 description 1
238000000527 sonication Methods 0.000 description 1
230000009870 specific binding Effects 0.000 description 1
230000002269 spontaneous effect Effects 0.000 description 1
238000007619 statistical method Methods 0.000 description 1
230000000638 stimulation Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
238000003860 storage Methods 0.000 description 1
238000007920 subcutaneous administration Methods 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
230000002459 sustained effect Effects 0.000 description 1
230000002381 testicular Effects 0.000 description 1
ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 1
210000003684 theca cell Anatomy 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
238000001890 transfection Methods 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
238000011870 unpaired t-test Methods 0.000 description 1
210000002700 urine Anatomy 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
239000003643 water by type Substances 0.000 description 1

Classifications

- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/689—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to pregnancy or the gonads

Landscapes

Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Immunology (AREA)
Chemical & Material Sciences (AREA)
Biomedical Technology (AREA)
Urology & Nephrology (AREA)
Hematology (AREA)
Biotechnology (AREA)
General Health & Medical Sciences (AREA)
Cell Biology (AREA)
Pathology (AREA)
Food Science & Technology (AREA)
Medicinal Chemistry (AREA)
Physics & Mathematics (AREA)
Analytical Chemistry (AREA)
Biochemistry (AREA)
Microbiology (AREA)
General Physics & Mathematics (AREA)
Endocrinology (AREA)
Gynecology & Obstetrics (AREA)
Pregnancy & Childbirth (AREA)
Reproductive Health (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

CA000531961A 1986-03-13 1987-03-13 Methode de dosage immunologique de l'inhibine Expired - Lifetime CA1307736C (fr)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
AUPH5019		1986-03-13
AUPH501986		1986-03-13

Publications (1)

Publication Number	Publication Date
CA1307736C true CA1307736C (fr)	1992-09-22

Family

ID=3771514

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA000531961A Expired - Lifetime CA1307736C (fr)	1986-03-13	1987-03-13	Methode de dosage immunologique de l'inhibine

Country Status (8)

Country	Link
EP (1)	EP0260306A4 (fr)
JP (1)	JPS63503086A (fr)
AU (1)	AU599373B2 (fr)
CA (1)	CA1307736C (fr)
IL (1)	IL81889A0 (fr)
NZ (1)	NZ219609A (fr)
WO (1)	WO1987005702A1 (fr)
ZA (1)	ZA871844B (fr)

Families Citing this family (19)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5942220A (en) *	1990-03-16	1999-08-24	Chiron Corporation	Inhibitor of cytokine activity and applications thereof
GB9224965D0 (en) *	1992-11-28	1993-01-20	Kodak Ltd	Antenatal screening for chromosomal abnormalities
GB9316369D0 (en) *	1993-08-06	1993-09-22	Surface Active Ltd	Diagnostic method
GB9410345D0 (en) *	1994-05-24	1994-07-13	Univ Oxford Brookes	Method of genetic testing
GB9606261D0 (en) *	1996-03-25	1996-05-29	Johnson & Johnson Clin Diag	Prenatal screening for fetal abnormalities
GB9614615D0 (en) *	1996-07-11	1996-09-04	Isis Innovation	Diagnosis of pre-eclampsia
US6620590B2 (en)	1996-07-11	2003-09-16	Isis Innovation Limited	Diagnosis of pre-eclampsia
JP2002537776A (ja)	1999-02-25	2002-11-12	オークランドユニサーヴィスィズリミテッド	早発性卵巣機能不全の診断及び治療
WO2004060403A2 (fr)	2003-01-06	2004-07-22	Angiochem Inc.	Methode de transport d'un compose a travers une barriere sang/cerveau
EP1616190A4 (fr) *	2003-03-28	2006-12-06	Univ Monash	Diagnostic de cancer a un stade avance
RU2408605C2 (ru)	2005-02-18	2011-01-10	Анджиокем Инк.	Полипептид, способный преодолевать гематоэнцефалический барьер, и его конъюгат
ES2744225T3 (es)	2005-07-15	2020-02-24	Angiochem Inc	Uso de polipéptidos de aprotinina como portadores en conjugados farmacéuticos
US9365634B2 (en)	2007-05-29	2016-06-14	Angiochem Inc.	Aprotinin-like polypeptides for delivering agents conjugated thereto to tissues
CA2740316A1 (fr)	2008-10-15	2010-04-22	Angiochem Inc.	Conjugues d'agonistes de glp-1 et leurs utilisations
CA2745524C (fr)	2008-12-05	2020-06-09	Angiochem Inc.	Conjugues de neurotensine ou d'analogues de neurotensine et leurs applications
US8853353B2 (en)	2008-12-17	2014-10-07	Angiochem, Inc.	Membrane type-1 matrix metalloprotein inhibitors and uses thereof
MX2011011023A (es)	2009-04-20	2012-01-20	Angiochem Inc	Tratamiento de cancer de ovarios usando un agente anti-cancer conjugado con un analogo de angiopep-2.
RU2012103240A (ru)	2009-07-02	2013-08-10	Ангиокем Инк.	Мультимерные пептидные конъюгаты и их применение
EP3307326B9 (fr)	2015-06-15	2021-02-24	Angiochem Inc.	Procédés de traitement d'une carcinomatose leptoméningée

Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1341617C (fr) *	1984-06-08	2011-06-28	Henry George Burger	Inhibine extracte de liquide folliculaire ovarien
KR940004077B1 (ko) *	1985-04-18	1994-05-11	바이오테크놀로지 오스트레일리아 프로프라이어터리 리밋티드	재조합 인히빈
US4624944A (en) *	1985-06-14	1986-11-25	The Regents Of The University Of California	Human seminal alpha-inhibins
US4740587A (en) *	1985-07-18	1988-04-26	The Salk Institute For Biological Studies	Inhibin and method of purifying same
NZ217727A (en) *	1985-10-03	1990-05-28	Genentech Inc	Nucleic acid encoding alpha or b chain of inhibin, its production and compositions containing it

1987
- 1987-03-13 AU AU72036/87A patent/AU599373B2/en not_active Ceased
- 1987-03-13 WO PCT/AU1987/000070 patent/WO1987005702A1/fr not_active Ceased
- 1987-03-13 EP EP19870902027 patent/EP0260306A4/en not_active Withdrawn
- 1987-03-13 ZA ZA871844A patent/ZA871844B/xx unknown
- 1987-03-13 JP JP62502014A patent/JPS63503086A/ja active Pending
- 1987-03-13 NZ NZ219609A patent/NZ219609A/xx unknown
- 1987-03-13 CA CA000531961A patent/CA1307736C/fr not_active Expired - Lifetime
- 1987-03-13 IL IL81889A patent/IL81889A0/xx unknown

Also Published As

Publication number	Publication date
EP0260306A1 (fr)	1988-03-23
EP0260306A4 (en)	1990-09-26
IL81889A0 (en)	1987-10-20
WO1987005702A1 (fr)	1987-09-24
JPS63503086A (ja)	1988-11-10
NZ219609A (en)	1990-09-26
AU7203687A (en)	1987-10-09
AU599373B2 (en)	1990-07-19
ZA871844B (en)	1988-05-25

Legal Events

Date	Code	Title	Description
1997-09-22	MKLA	Lapsed

Publication	Publication Date	Title
CA1307736C (fr)	1992-09-22	Methode de dosage immunologique de l'inhibine
JP2521707B2 (ja)	1996-08-07	卵胞液から単離したインヒビン
McLachlan et al.	1986	The radioimmunoassay of bovine and human follicular fluid and serum inhibin
Jackson et al.	1985	Characterization of a large molecular weight prolactin in women with idiopathic hyperprolactinemia and normal menses
ELSON et al.	1984	Identification of epidermal growth factor-like activity in human male reproductive tissues and fluids
Cunnah et al.	1987	Measurement of circulating corticotrophin-releasing factor in man
Liotta et al.	1979	Biosynthesis in vitro of immunoreactive 31,000-dalton corticotropin/β-endorphin-like material by bovine hypothalamus
Shukovski et al.	1989	Circulating immunoreactive oxytocin during the human menstrual cycle comes from the pituitary and is estradiol dependent
Gagel et al.	1980	Establishment of a calcitonin-producing rat medullary thyroid carcinoma cell line. II. Secretory studies of the tumor and cells in culture
Laster	1977	A pregnancy-specific protein in the bovine uterus
Matsuo et al.	1993	Human early placental trophoblasts produce an epidermal growth factor-like substance in synergy with thyroid hormone
Clifton et al.	2000	Localization and characterization of urocortin during human pregnancy
Stalla et al.	1984	Ovine (o) and human (h) corticotrophin releasing factor (CRF) in man: CRF-stimulation and CRF-immunoreactivity
BENVENISTE et al.	1979	Circulating big human prolactin: conversion to small human prolactin by reduction of disulfide bonds
Currie et al.	1977	Caprine placental lactogen: levels of prolactin-like and growth hormone-like activities in the circulation of pregnant goats determined by radioreceptor assays
Torkkeli et al.	1977	Hormonal regulation of uterine blastokinin synthesis and occurrence of blastokinin-like antigens in nonuterine tissues
US4489166A (en)	1984-12-18	Monitoring of human endometrial function by radioimmunoassay of PEP
Norman et al.	1968	Radioimmunoassay studies with human growth hormone and a pituitary lipid mobilizing factor
Ciarochi et al.	1985	Isolation and localization of neurophysin-like proteins in rat uterus
EP0178841B1 (fr)	1991-01-23	Protéine régulatrice des gonades
AU636318B2 (en)	1993-04-29	Inhibin isolated from ovarian follicular fluid
Cannon et al.	1998	Menstrual-and gender-dependent variations in circulating IL-1 agonists, antagonists, and binding proteins
NAKAZAWA et al.	1984	Immunohistochemical study on oxytocin-like substance in the human placenta
NISHIMURA et al.	1982	The characterization of alpha-subunit of glycoprotein hormone produced by undifferentiated carcinoma
Sinosich et al.	1991	Radioimmunoassay of inhibin based on synthetic human inhibin alpha-chain peptide