CA1077420A - Thymidine phosphorylase dans une preparation stabilisee - Google Patents

Thymidine phosphorylase dans une preparation stabilisee

Info

Publication number: CA1077420A
Authority: CA; Canada
Prior art keywords: enzyme; preparation; thymidine; thymidine phosphorylase; purified
Prior art date: 1975-01-27
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

CA331,779A

Other languages

English (en)

Inventor

Stanley R. M. Bushby

Thomas A. Krenitsky

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.)

Wellcome Foundation Ltd

Original Assignee

Wellcome Foundation 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.)

1975-01-27

Filing date

1979-07-13

Publication date

1980-05-13

1975-01-27 Priority claimed from GB3445/75A external-priority patent/GB1513461A/en

1979-07-13 Application filed by Wellcome Foundation Ltd filed Critical Wellcome Foundation Ltd

1979-07-13 Priority to CA331,779A priority Critical patent/CA1077420A/fr

1980-05-13 Application granted granted Critical

1980-05-13 Publication of CA1077420A publication Critical patent/CA1077420A/fr

Status Expired legal-status Critical Current

Links

102000013537 Thymidine Phosphorylase Human genes 0.000 title claims abstract description 26
101710132082 Pyrimidine/purine nucleoside phosphorylase Proteins 0.000 title claims abstract description 24
238000002360 preparation method Methods 0.000 title claims description 17
102000004190 Enzymes Human genes 0.000 claims abstract description 47
108090000790 Enzymes Proteins 0.000 claims abstract description 47
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims abstract description 13
229910052921 ammonium sulfate Inorganic materials 0.000 claims abstract description 13
235000011130 ammonium sulphate Nutrition 0.000 claims abstract description 13
241000588724 Escherichia coli Species 0.000 claims abstract description 10
239000001166 ammonium sulphate Substances 0.000 claims abstract description 7
239000008363 phosphate buffer Substances 0.000 claims abstract description 6
102000004169 proteins and genes Human genes 0.000 claims abstract description 6
108090000623 proteins and genes Proteins 0.000 claims abstract description 6
239000008057 potassium phosphate buffer Substances 0.000 claims description 8
239000000872 buffer Substances 0.000 claims description 7
230000000087 stabilizing effect Effects 0.000 claims 1
238000000034 method Methods 0.000 abstract description 19
230000001580 bacterial effect Effects 0.000 abstract description 17
238000000502 dialysis Methods 0.000 abstract description 7
239000000284 extract Substances 0.000 abstract description 6
238000010828 elution Methods 0.000 abstract description 4
238000005194 fractionation Methods 0.000 abstract description 4
238000001179 sorption measurement Methods 0.000 abstract description 4
239000012736 aqueous medium Substances 0.000 abstract description 3
238000004440 column chromatography Methods 0.000 abstract description 2
IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 31
230000000694 effects Effects 0.000 description 21
DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 16
IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 16
239000002609 medium Substances 0.000 description 16
229940104230 thymidine Drugs 0.000 description 16
RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 14
239000008280 blood Substances 0.000 description 13
210000004369 blood Anatomy 0.000 description 13
241000894006 Bacteria Species 0.000 description 12
238000012360 testing method Methods 0.000 description 12
229920001817 Agar Polymers 0.000 description 10
239000008272 agar Substances 0.000 description 10
239000000499 gel Substances 0.000 description 9
IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 description 9
229940079593 drug Drugs 0.000 description 8
239000003814 drug Substances 0.000 description 8
229960001082 trimethoprim Drugs 0.000 description 8
230000003432 anti-folate effect Effects 0.000 description 7
229940127074 antifolate Drugs 0.000 description 7
239000004052 folic acid antagonist Substances 0.000 description 7
239000001963 growth medium Substances 0.000 description 7
230000005764 inhibitory process Effects 0.000 description 7
239000000203 mixture Substances 0.000 description 7
238000000746 purification Methods 0.000 description 7
230000035945 sensitivity Effects 0.000 description 7
239000000725 suspension Substances 0.000 description 7
229940113082 thymine Drugs 0.000 description 7
239000001506 calcium phosphate Substances 0.000 description 6
229910000389 calcium phosphate Inorganic materials 0.000 description 6
235000011010 calcium phosphates Nutrition 0.000 description 6
239000000243 solution Substances 0.000 description 6
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 6
239000001913 cellulose Substances 0.000 description 5
229920002678 cellulose Polymers 0.000 description 5
229960005404 sulfamethoxazole Drugs 0.000 description 5
JLKIGFTWXXRPMT-UHFFFAOYSA-N sulphamethoxazole Chemical compound O1C(C)=CC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1 JLKIGFTWXXRPMT-UHFFFAOYSA-N 0.000 description 5
GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 4
230000007423 decrease Effects 0.000 description 4
238000002156 mixing Methods 0.000 description 4
150000003456 sulfonamides Chemical class 0.000 description 4
230000015572 biosynthetic process Effects 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
239000003795 chemical substances by application Substances 0.000 description 3
238000001802 infusion Methods 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
239000007787 solid Substances 0.000 description 3
239000008174 sterile solution Substances 0.000 description 3
WZRJTRPJURQBRM-UHFFFAOYSA-N 4-amino-n-(5-methyl-1,2-oxazol-3-yl)benzenesulfonamide;5-[(3,4,5-trimethoxyphenyl)methyl]pyrimidine-2,4-diamine Chemical compound O1C(C)=CC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1.COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 WZRJTRPJURQBRM-UHFFFAOYSA-N 0.000 description 2
ALYNCZNDIQEVRV-UHFFFAOYSA-N 4-aminobenzoic acid Chemical compound NC1=CC=C(C(O)=O)C=C1 ALYNCZNDIQEVRV-UHFFFAOYSA-N 0.000 description 2
241000193385 Geobacillus stearothermophilus Species 0.000 description 2
CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
102000009097 Phosphorylases Human genes 0.000 description 2
108010073135 Phosphorylases Proteins 0.000 description 2
OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
238000003556 assay Methods 0.000 description 2
239000011575 calcium Substances 0.000 description 2
229940047766 co-trimoxazole Drugs 0.000 description 2
238000001816 cooling Methods 0.000 description 2
239000000287 crude extract Substances 0.000 description 2
239000012530 fluid Substances 0.000 description 2
235000019152 folic acid Nutrition 0.000 description 2
238000009472 formulation Methods 0.000 description 2
238000011534 incubation Methods 0.000 description 2
239000006166 lysate Substances 0.000 description 2
239000008188 pellet Substances 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
239000000126 substance Substances 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
238000005406 washing Methods 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
241000193755 Bacillus cereus Species 0.000 description 1
208000035143 Bacterial infection Diseases 0.000 description 1
238000009631 Broth culture Methods 0.000 description 1
239000002126 C01EB10 - Adenosine Substances 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
241000588919 Citrobacter freundii Species 0.000 description 1
241000588914 Enterobacter Species 0.000 description 1
241000186811 Erysipelothrix Species 0.000 description 1
241000606768 Haemophilus influenzae Species 0.000 description 1
241000588747 Klebsiella pneumoniae Species 0.000 description 1
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
241001465754 Metazoa Species 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
241000588769 Proteus <enterobacteria> Species 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
241000607142 Salmonella Species 0.000 description 1
241000405383 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 Species 0.000 description 1
241000277284 Salvelinus fontinalis Species 0.000 description 1
241000607715 Serratia marcescens Species 0.000 description 1
241000191967 Staphylococcus aureus Species 0.000 description 1
241000194017 Streptococcus Species 0.000 description 1
GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
241000251539 Vertebrata <Metazoa> Species 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
239000002250 absorbent Substances 0.000 description 1
230000002745 absorbent Effects 0.000 description 1
239000002253 acid Substances 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
229960005305 adenosine Drugs 0.000 description 1
239000003463 adsorbent Substances 0.000 description 1
229960004050 aminobenzoic acid Drugs 0.000 description 1
238000002829 antibacterial sensitivity test Methods 0.000 description 1
239000004599 antimicrobial Substances 0.000 description 1
208000022362 bacterial infectious disease Diseases 0.000 description 1
230000008033 biological extinction Effects 0.000 description 1
210000004556 brain Anatomy 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
229910052799 carbon Inorganic materials 0.000 description 1
239000006285 cell suspension Substances 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
238000000354 decomposition reaction Methods 0.000 description 1
238000009792 diffusion process Methods 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
229910000397 disodium phosphate Inorganic materials 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
229940014144 folate Drugs 0.000 description 1
OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 1
239000011724 folic acid Substances 0.000 description 1
150000002224 folic acids Chemical class 0.000 description 1
230000005484 gravity Effects 0.000 description 1
229940047650 haemophilus influenzae Drugs 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
230000002452 interceptive effect Effects 0.000 description 1
238000002955 isolation Methods 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
229910052943 magnesium sulfate Inorganic materials 0.000 description 1
235000019341 magnesium sulphate Nutrition 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
238000012544 monitoring process Methods 0.000 description 1
229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
230000003472 neutralizing effect Effects 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
238000000424 optical density measurement Methods 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
230000003389 potentiating effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
150000003212 purines Chemical class 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
230000007017 scission Effects 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
238000000527 sonication Methods 0.000 description 1
241000894007 species Species 0.000 description 1
239000013589 supplement Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

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Enzymes And Modification Thereof (AREA)

CA331,779A 1975-01-27 1979-07-13 Thymidine phosphorylase dans une preparation stabilisee Expired CA1077420A (fr)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
CA331,779A CA1077420A (fr)	1975-01-27	1979-07-13	Thymidine phosphorylase dans une preparation stabilisee

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
GB3445/75A GB1513461A (en)	1975-01-27	1975-01-27	Bacterial culture medium
CA244,671A CA1077379A (fr)	1975-01-27	1976-01-27	Milieu de culture bacteriologique
CA331,779A CA1077420A (fr)	1975-01-27	1979-07-13	Thymidine phosphorylase dans une preparation stabilisee

Publications (1)

Publication Number	Publication Date
CA1077420A true CA1077420A (fr)	1980-05-13

Family

ID=27164307

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA331,779A Expired CA1077420A (fr)	1975-01-27	1979-07-13	Thymidine phosphorylase dans une preparation stabilisee

Country Status (1)

Country	Link
CA (1)	CA1077420A (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2188234C2 (ru) *	2000-08-11	2002-08-27	Институт биоорганической химии им. М.М.Шемякина и Ю.А.Овчинникова РАН	Способ получения рекомбинантной тимидин-фосфорилазы, рекомбинантная плазмидная днк pertpho1 и штамм escherichia coli bl21(de3)/pertpho1-продуцент тимидин-форфорилазы

1979
- 1979-07-13 CA CA331,779A patent/CA1077420A/fr not_active Expired

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2188234C2 (ru) *	2000-08-11	2002-08-27	Институт биоорганической химии им. М.М.Шемякина и Ю.А.Овчинникова РАН	Способ получения рекомбинантной тимидин-фосфорилазы, рекомбинантная плазмидная днк pertpho1 и штамм escherichia coli bl21(de3)/pertpho1-продуцент тимидин-форфорилазы

Legal Events

Date	Code	Title	Description
1997-05-13	MKEX	Expiry

Publication	Publication Date	Title
Jameson et al.	1980	Inhibition of microtubule assembly by phosphorylation of microtubule-associated proteins
DeMoss	1955	[43] Glucose-6-phosphate and 6-phosphogluconic dehydrogenases from Leuconostoc mesenteroides
Ferone et al.	1975	Identification of Harper-Cawston factor as thymidine phosphorylase and removal from media of substances interfering with susceptibility testing to sulfonamides and diaminopyrimidines
Rhuland	1957	Role of α, ε-diaminopimelic acid in the cellular integrity of Escherichia coli
Wolf et al.	1977	Purification and properties of high-affinity Ca2+-ATPase of human erythrocyte membranes.
Labow et al.	1966	Crystalline D-serine dehydrase
CA1194433A (fr)	1985-10-01	PROCEDE DE PRODUCTION D'UN MICROORGANISME PRODUISANT DE .alpha.-GALACTOSIDASE SANS INVERTASE, MICROORGANISME UTILISE A CETTE FIN ET SON UTILISATION
CA1077379A (fr)	1980-05-13	Milieu de culture bacteriologique
US4309502A (en)	1982-01-05	Enzymatic assay for glycerol and triglycerides and a reagent for use therein
CA1077420A (fr)	1980-05-13	Thymidine phosphorylase dans une preparation stabilisee
US4178212A (en)	1979-12-11	Stabilized thymidine phosphorylase formulation
Nakayama et al.	1972	Biosynthetic pathway of thiamine pyrophosphate: a special reference to the thiamine monophosphate-requiring mutant and the thiamine pyrophosphate-requiring mutant of Escherichia coli
US3669843A (en)	1972-06-13	Process for the production of uricase
EP0218863B1 (fr)	1992-04-15	D(-)-mandélate déshydrogénase produite par voie microbiologique, procédé pour son obtention et son utilisation
US4304864A (en)	1981-12-08	Long-chain acyl-coenzyme-A synthetase
Griffiths et al.	1990	Characterization of Aeromonas salmonicida variants with altered cell surfaces and their use in studying surface protein assembly
US4927753A (en)	1990-05-22	Quantitative determination of L-fucose
Wickus et al.	1973	Partial purification and properties of the pyruvate-uridine diphospho-N-acetylglucosamine transferase from Staphylococcus epidermidis
Knichel et al.	1982	d‐Malic Enzyme of Pseudomonas fluorescens
CA1112193A (fr)	1981-11-10	Preparation stabilisee
Porter et al.	1977	Partial purification and characterization of citrate synthase from Dictyostelium discoideum
JP3029915B2 (ja)	2000-04-10	耐熱性アデノシン−５’−ホスホスルフェートキナーゼ及びその製造法
CA1086670A (fr)	1980-09-30	.beta.-GALACTOSIDASE
Breeze et al.	1982	An improved method using acetyl‐coenzyme A regeneration for the enzymic inactivation of aminoglycosides prior to sterility testing
JP3078067B2 (ja)	2000-08-21	耐熱性アデノシン−５’−３リン酸スルフリラーゼ及びその製造法

CA1077420A - Thymidine phosphorylase dans une preparation stabilisee - Google Patents

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Priority Applications (1)

Applications Claiming Priority (3)

Publications (1)

Family

ID=27164307

Family Applications (1)

Country Status (1)

Cited By (1)

Cited By (1)

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