JPS6140067B2 - - Google Patents

Info

Publication number: JPS6140067B2
Authority: JP; Japan
Prior art keywords: antibody; acid; antibodies; charge; amino compound
Prior art date: 1978-05-29
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

Application number

JP53063326A

Other languages

English (en)

Japanese (ja)

Other versions

JPS54155094A (en

Inventor

Taku Ogura

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.)

Seikagaku Corp

Original Assignee

Seikagaku Corp

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.)

1978-05-29

Filing date

1978-05-29

Publication date

1986-09-06

1978-05-29 Application filed by Seikagaku Corp filed Critical Seikagaku Corp

1978-05-29 Priority to JP6332678A priority Critical patent/JPS54155094A/ja

1979-12-06 Publication of JPS54155094A publication Critical patent/JPS54155094A/ja

1986-09-06 Publication of JPS6140067B2 publication Critical patent/JPS6140067B2/ja

Status Granted legal-status Critical Current

Links

-1 amino compound Chemical class 0.000 claims description 15
238000000034 method Methods 0.000 claims description 15
230000002378 acidificating effect Effects 0.000 claims description 12
KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 claims description 11
150000003839 salts Chemical class 0.000 claims description 9
238000000760 immunoelectrophoresis Methods 0.000 description 11
229920001817 Agar Polymers 0.000 description 9
239000008272 agar Substances 0.000 description 9
238000001962 electrophoresis Methods 0.000 description 8
102000009027 Albumins Human genes 0.000 description 7
108010088751 Albumins Proteins 0.000 description 7
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
239000000427 antigen Substances 0.000 description 6
102000036639 antigens Human genes 0.000 description 6
108091007433 antigens Proteins 0.000 description 6
238000001155 isoelectric focusing Methods 0.000 description 5
FTOAOBMCPZCFFF-UHFFFAOYSA-N 5,5-diethylbarbituric acid Chemical compound CCC1(CC)C(=O)NC(=O)NC1=O FTOAOBMCPZCFFF-UHFFFAOYSA-N 0.000 description 4
102000008100 Human Serum Albumin Human genes 0.000 description 4
108091006905 Human Serum Albumin Proteins 0.000 description 4
239000002953 phosphate buffered saline Substances 0.000 description 4
239000002244 precipitate Substances 0.000 description 4
KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 4
JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 4
239000000243 solution Substances 0.000 description 4
XOAAWQZATWQOTB-UHFFFAOYSA-N taurine Chemical compound NCCS(O)(=O)=O XOAAWQZATWQOTB-UHFFFAOYSA-N 0.000 description 4
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
230000015572 biosynthetic process Effects 0.000 description 3
239000000872 buffer Substances 0.000 description 3
235000018102 proteins Nutrition 0.000 description 3
102000004169 proteins and genes Human genes 0.000 description 3
108090000623 proteins and genes Proteins 0.000 description 3
IIACRCGMVDHOTQ-UHFFFAOYSA-N sulfamic acid Chemical class NS(O)(=O)=O IIACRCGMVDHOTQ-UHFFFAOYSA-N 0.000 description 3
PIICEJLVQHRZGT-UHFFFAOYSA-N Ethylenediamine Chemical compound NCCN PIICEJLVQHRZGT-UHFFFAOYSA-N 0.000 description 2
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
DRBBFCLWYRJSJZ-UHFFFAOYSA-N N-phosphocreatine Chemical compound OC(=O)CN(C)C(=N)NP(O)(O)=O DRBBFCLWYRJSJZ-UHFFFAOYSA-N 0.000 description 2
JZTPOMIFAFKKSK-UHFFFAOYSA-N O-phosphonohydroxylamine Chemical class NOP(O)(O)=O JZTPOMIFAFKKSK-UHFFFAOYSA-N 0.000 description 2
241000283973 Oryctolagus cuniculus Species 0.000 description 2
239000008351 acetate buffer Substances 0.000 description 2
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
229910052921 ammonium sulfate Inorganic materials 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
239000007864 aqueous solution Substances 0.000 description 2
235000003704 aspartic acid Nutrition 0.000 description 2
229960002319 barbital Drugs 0.000 description 2
MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 2
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
239000007795 chemical reaction product Substances 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
150000002337 glycosamines Chemical class 0.000 description 2
239000000203 mixture Substances 0.000 description 2
229920000768 polyamine Polymers 0.000 description 2
238000004445 quantitative analysis Methods 0.000 description 2
210000002966 serum Anatomy 0.000 description 2
ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 2
PFNFFQXMRSDOHW-UHFFFAOYSA-N spermine Chemical compound NCCCNCCCCNCCCN PFNFFQXMRSDOHW-UHFFFAOYSA-N 0.000 description 2
229960003080 taurine Drugs 0.000 description 2
HALGLMAADGHVSV-UHFFFAOYSA-N 1-aminopropane-2-sulfonic acid Chemical compound NCC(C)S(O)(=O)=O HALGLMAADGHVSV-UHFFFAOYSA-N 0.000 description 1
MSWZFWKMSRAUBD-GASJEMHNSA-N 2-amino-2-deoxy-D-galactopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O MSWZFWKMSRAUBD-GASJEMHNSA-N 0.000 description 1
MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 1
ZMCHBSMFKQYNKA-UHFFFAOYSA-N 2-aminobenzenesulfonic acid Chemical compound NC1=CC=CC=C1S(O)(=O)=O ZMCHBSMFKQYNKA-UHFFFAOYSA-N 0.000 description 1
XDZZQMNDCFNREN-UHFFFAOYSA-N 2-azaniumylpropane-1-sulfonate Chemical compound CC(N)CS(O)(=O)=O XDZZQMNDCFNREN-UHFFFAOYSA-N 0.000 description 1
BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
SNKZJIOFVMKAOJ-UHFFFAOYSA-N 3-Aminopropanesulfonate Chemical compound NCCCS(O)(=O)=O SNKZJIOFVMKAOJ-UHFFFAOYSA-N 0.000 description 1
QRAXZXPSAGQUNP-UHFFFAOYSA-N 4-(methylamino)benzenesulfonic acid Chemical compound CNC1=CC=C(S(O)(=O)=O)C=C1 QRAXZXPSAGQUNP-UHFFFAOYSA-N 0.000 description 1
HVBSAKJJOYLTQU-UHFFFAOYSA-N 4-aminobenzenesulfonic acid Chemical compound NC1=CC=C(S(O)(=O)=O)C=C1 HVBSAKJJOYLTQU-UHFFFAOYSA-N 0.000 description 1
KNILZINKISHVIQ-UHFFFAOYSA-N 4-azaniumylbutane-1-sulfonate Chemical compound NCCCCS(O)(=O)=O KNILZINKISHVIQ-UHFFFAOYSA-N 0.000 description 1
SKCBPEVYGOQGJN-TXICZTDVSA-N 5-phospho-beta-D-ribosylamine Chemical compound N[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O SKCBPEVYGOQGJN-TXICZTDVSA-N 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
241000283707 Capra Species 0.000 description 1
241000700198 Cavia Species 0.000 description 1
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
241000282412 Homo Species 0.000 description 1
WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
241001465754 Metazoa Species 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
241001494479 Pecora Species 0.000 description 1
239000005700 Putrescine Substances 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
239000002253 acid Substances 0.000 description 1
GFFGJBXGBJISGV-UHFFFAOYSA-N adenyl group Chemical group N1=CN=C2N=CNC2=C1N GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
235000001014 amino acid Nutrition 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
125000003277 amino group Chemical group 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
ILFFFKFZHRGICY-UHFFFAOYSA-N anthracene-1-sulfonic acid Chemical compound C1=CC=C2C=C3C(S(=O)(=O)O)=CC=CC3=CC2=C1 ILFFFKFZHRGICY-UHFFFAOYSA-N 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
159000000007 calcium salts Chemical class 0.000 description 1
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
229920002301 cellulose acetate Polymers 0.000 description 1
239000003638 chemical reducing agent Substances 0.000 description 1
238000004440 column chromatography Methods 0.000 description 1
OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical group NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 1
238000004042 decolorization Methods 0.000 description 1
150000004985 diamines Chemical class 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
239000003814 drug Substances 0.000 description 1
239000000834 fixative Substances 0.000 description 1
239000000499 gel Substances 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
229960002442 glucosamine Drugs 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical group O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
210000002414 leg Anatomy 0.000 description 1
239000012528 membrane Substances 0.000 description 1
239000002773 nucleotide Substances 0.000 description 1
125000003729 nucleotide group Chemical group 0.000 description 1
229920001542 oligosaccharide Polymers 0.000 description 1
150000002482 oligosaccharides Chemical class 0.000 description 1
235000021317 phosphate Nutrition 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
150000003014 phosphoric acid esters Chemical class 0.000 description 1
159000000001 potassium salts Chemical class 0.000 description 1
238000005185 salting out Methods 0.000 description 1
239000012279 sodium borohydride Substances 0.000 description 1
229910000033 sodium borohydride Inorganic materials 0.000 description 1
159000000000 sodium salts Chemical class 0.000 description 1
229940063673 spermidine Drugs 0.000 description 1
229940063675 spermine Drugs 0.000 description 1
239000000126 substance Substances 0.000 description 1
229950000244 sulfanilic acid Drugs 0.000 description 1
QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
DPJRMOMPQZCRJU-UHFFFAOYSA-M thiamine hydrochloride Chemical compound Cl.[Cl-].CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N DPJRMOMPQZCRJU-UHFFFAOYSA-M 0.000 description 1
YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
210000000689 upper leg Anatomy 0.000 description 1
239000011691 vitamin B1 Substances 0.000 description 1
238000005406 washing Methods 0.000 description 1

Landscapes

Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)

JP6332678A 1978-05-29 1978-05-29 Method of changing electrical charge of antibody Granted JPS54155094A (en)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP6332678A JPS54155094A (en)	1978-05-29	1978-05-29	Method of changing electrical charge of antibody

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP6332678A JPS54155094A (en)	1978-05-29	1978-05-29	Method of changing electrical charge of antibody

Publications (2)

Publication Number	Publication Date
JPS54155094A JPS54155094A (en)	1979-12-06
JPS6140067B2 true JPS6140067B2 (de)	1986-09-06

Family

ID=13226011

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP6332678A Granted JPS54155094A (en)	1978-05-29	1978-05-29	Method of changing electrical charge of antibody

Country Status (1)

Country	Link
JP (1)	JPS54155094A (de)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4287300A (en) *	1979-07-26	1981-09-01	Syva Company	Charge effects in enzyme immunoassays
CA1203164A (en)	1982-03-09	1986-04-15	Thomas J. Mckearn	Antibody conjugates
US5140104A (en) *	1982-03-09	1992-08-18	Cytogen Corporation	Amine derivatives of folic acid analogs
US4741900A (en) *	1982-11-16	1988-05-03	Cytogen Corporation	Antibody-metal ion complexes
US4868132A (en) *	1987-02-03	1989-09-19	Abbott Laboratories	Fluorescence polarization immunoassay for amphetamine/methamphetamine

1978
- 1978-05-29 JP JP6332678A patent/JPS54155094A/ja active Granted

Also Published As

Publication number	Publication date
JPS54155094A (en)	1979-12-06

Publication	Publication Date	Title
Wofsy et al.	1963	Effects of the amidination reaction on antibody activity and on the physical properties of some proteins
Yonemasu et al.	1972	Structural studies on human Clq: non-covalent and covalent subunits
CA1242393A (en)	1988-09-27	Digitalis antibodies, process for the preparation thereof and the use thereof for the therapy of digitalis intoxications
EP0346087A2 (de)	1989-12-13	Hybride Antikörper und Verfahren zu ihrer Herstellung
Holt et al.	1975	Immunological approach to the role of the low-molecular-weight subunits in myosin. II. Interaction of myosin and its subfragments with antibodies to the light chains
JPS6361319B2 (de)	1988-11-28
FR2464995A1 (fr)	1981-03-20	Procede de preparation d'une sous-population virale ayant une sensibilite accrue envers des cellules-hotes du virus et applications de cette sous-population
JPS6140067B2 (de)	1986-09-06
Wright et al.	1977	The interaction of protein A and Fc fragment of rabbit immunoglobulin G as probed by complement-fixation and nuclear-magnetic-resonance studies
JPS60260519A (ja)	1985-12-23	組織蛋白ｐｐ↓１↓８、その取得方法およびその用途
JPH0550520B2 (de)	1993-07-29
JPH0694716A (ja)	1994-04-08	免疫測定法
JPH01144993A (ja)	1989-06-07	ＨＢｓ抗原測定のための方法、ハイブリドーマ、モノクローナル抗体および感作血球
SU1158029A3 (ru)	1985-05-23	Способ количественного определени трийодтиронина
CN118005797B (zh)	2024-07-19	一种抗人碱性磷酸酶单克隆抗体及其在免疫类诊断试剂阻断剂制备中的应用
McDonald et al.	1979	Purification of the subunit Clq from the first component of equine complement
JPH07122622B2 (ja)	1995-12-25	免疫センサ−
Shainoff et al.	1981	Cascade immunoelectrophoresis: Combined electrophoretic and solid-phase processing of immunoreactive protein by zonal immobilization
KAGIYAMA et al.	1968	The Binding Mechanism of Haptoglobin with Hemoglobin. III Immunochemical Characterization of the Intermediate and Saturated Forms of Hemoglobin-Haptoglobin 1-1 Complex
JP2002243732A (ja)	2002-08-28	新規な抗体及び該抗体を含む免疫試薬
JPS6283665A (ja)	1987-04-17	ヒト癌胎児性抗原の免疫化学的測定法および試薬
JPH10332693A (ja)	1998-12-18	被検体の前処理方法
JPH01269485A (ja)	1989-10-26	モノクローナル抗体産生細胞ラインおよびモノクローナル抗体
JPS62258399A (ja)	1987-11-10	Ｃ−反応性蛋白質の精製方法
GM et al.	1961	Studies on structural units of the gamma-globulins.