CA1230300A - Stabilized isoenzyme control product - Google Patents

Stabilized isoenzyme control product

Info

Publication number: CA1230300A
Authority: CA; Canada
Prior art keywords: reagent; stabilizing means; lactose; isoenzyme; plexiform
Prior art date: 1983-06-06
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

CA000453361A

Other languages

English (en)

French (fr)

Inventor

Michael K. Hoskins

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.)

Bio Rad Laboratories Inc

Original Assignee

Individual

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.)

1983-06-06

Filing date

1984-05-02

Publication date

1987-12-15

1984-05-02 Application filed by Individual filed Critical Individual

1987-12-15 Application granted granted Critical

1987-12-15 Publication of CA1230300A publication Critical patent/CA1230300A/en

Status Expired legal-status Critical Current

Links

108010044467 Isoenzymes Proteins 0.000 title claims abstract description 77
230000000087 stabilizing effect Effects 0.000 claims abstract description 73
239000003153 chemical reaction reagent Substances 0.000 claims abstract description 70
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 claims abstract description 30
239000008101 lactose Substances 0.000 claims abstract description 30
235000000346 sugar Nutrition 0.000 claims abstract description 22
238000000034 method Methods 0.000 claims abstract description 11
239000002738 chelating agent Substances 0.000 claims abstract description 5
150000008163 sugars Chemical class 0.000 claims abstract description 3
102000004190 Enzymes Human genes 0.000 claims description 27
108090000790 Enzymes Proteins 0.000 claims description 27
230000000694 effects Effects 0.000 claims description 26
230000008707 rearrangement Effects 0.000 claims description 21
-1 monosaccharide sugars Chemical class 0.000 claims description 19
GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 claims description 17
GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 claims description 17
OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims description 16
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 claims description 16
GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims description 16
229930195725 Mannitol Natural products 0.000 claims description 16
239000000594 mannitol Substances 0.000 claims description 16
235000010355 mannitol Nutrition 0.000 claims description 16
GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 claims description 15
239000007864 aqueous solution Substances 0.000 claims description 10
108090000623 proteins and genes Proteins 0.000 claims description 10
102000004169 proteins and genes Human genes 0.000 claims description 9
239000000243 solution Substances 0.000 claims description 8
150000001455 metallic ions Chemical class 0.000 claims description 6
229910019142 PO4 Inorganic materials 0.000 claims description 4
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 4
239000010452 phosphate Substances 0.000 claims description 4
230000000845 anti-microbial effect Effects 0.000 claims 1
230000002401 inhibitory effect Effects 0.000 claims 1
230000000813 microbial effect Effects 0.000 claims 1
150000002016 disaccharides Chemical class 0.000 abstract description 2
150000002772 monosaccharides Chemical class 0.000 abstract description 2
102000003855 L-lactate dehydrogenase Human genes 0.000 description 12
108700023483 L-lactate dehydrogenases Proteins 0.000 description 12
210000001519 tissue Anatomy 0.000 description 12
239000000047 product Substances 0.000 description 9
238000007710 freezing Methods 0.000 description 7
230000008014 freezing Effects 0.000 description 7
235000018102 proteins Nutrition 0.000 description 5
239000000470 constituent Substances 0.000 description 4
DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 4
239000000463 material Substances 0.000 description 4
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
102100036475 Alanine aminotransferase 1 Human genes 0.000 description 2
108010082126 Alanine transaminase Proteins 0.000 description 2
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
108700016171 Aspartate ammonia-lyases Proteins 0.000 description 2
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical class O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
108090000340 Transaminases Proteins 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
229940109239 creatinine Drugs 0.000 description 2
238000001914 filtration Methods 0.000 description 2
238000004108 freeze drying Methods 0.000 description 2
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
230000004060 metabolic process Effects 0.000 description 2
239000000203 mixture Substances 0.000 description 2
210000003205 muscle Anatomy 0.000 description 2
108090000765 processed proteins & peptides Proteins 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
238000000926 separation method Methods 0.000 description 2
102000014898 transaminase activity proteins Human genes 0.000 description 2
229930024421 Adenine Natural products 0.000 description 1
GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
229910002012 Aerosil® Inorganic materials 0.000 description 1
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical group OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
101710107035 Gamma-glutamyltranspeptidase Proteins 0.000 description 1
108010024636 Glutathione Proteins 0.000 description 1
101710173228 Glutathione hydrolase proenzyme Proteins 0.000 description 1
OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
108091000080 Phosphotransferase Proteins 0.000 description 1
102000001253 Protein Kinase Human genes 0.000 description 1
LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 1
229960000643 adenine Drugs 0.000 description 1
235000001014 amino acid Nutrition 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
210000004556 brain Anatomy 0.000 description 1
230000000747 cardiac effect Effects 0.000 description 1
230000003197 catalytic effect Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
230000004069 differentiation Effects 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
230000005496 eutectics Effects 0.000 description 1
239000012467 final product Substances 0.000 description 1
102000006640 gamma-Glutamyltransferase Human genes 0.000 description 1
230000008571 general function Effects 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
229960003180 glutathione Drugs 0.000 description 1
238000000227 grinding Methods 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
238000002955 isolation Methods 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
210000004185 liver Anatomy 0.000 description 1
230000007774 longterm Effects 0.000 description 1
238000012423 maintenance Methods 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
230000002107 myocardial effect Effects 0.000 description 1
210000000056 organ Anatomy 0.000 description 1
229910052698 phosphorus Inorganic materials 0.000 description 1
239000011574 phosphorus Substances 0.000 description 1
102000020233 phosphotransferase Human genes 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
239000000843 powder Substances 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
108060006633 protein kinase Proteins 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
230000000241 respiratory effect Effects 0.000 description 1
241000894007 species Species 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
238000012360 testing method Methods 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1

Landscapes

Enzymes And Modification Thereof (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Fats And Perfumes (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)
Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)

CA000453361A 1983-06-06 1984-05-02 Stabilized isoenzyme control product Expired CA1230300A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US50121383A	1983-06-06	1983-06-06
US501,213		1983-06-06

Publications (1)

Publication Number	Publication Date
CA1230300A true CA1230300A (en)	1987-12-15

Family

ID=23992572

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA000453361A Expired CA1230300A (en)	1983-06-06	1984-05-02	Stabilized isoenzyme control product

Country Status (6)

Country	Link
JP (1)	JP2596911B2 (da)
AU (1)	AU583474B2 (da)
CA (1)	CA1230300A (da)
DK (1)	DK275184A (da)
IL (1)	IL72030A0 (da)
NO (1)	NO842258L (da)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1226795A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized coagulation control products
CA1226794A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized multiparameter control product
US4663295A (en) *	1983-06-29	1987-05-05	Ciba Corning Diagnostics Corp.	Estrogen-progesterone control reagents and methods for making same
JP2575648B2 (ja) *	1986-04-24	1997-01-29	国際試薬株式会社	クレアチンキナ−ゼの安定化方法
IT1394539B1 (it) *	2009-05-19	2012-07-05	Sentinel Ch S P A	Uso di uno stabilizzante delle polimerasi per la liofilizzazione e la preparazione di kit pronti per l'uso

Family Cites Families (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS4834912A (da) *	1971-09-09	1973-05-23
JPS589688A (ja) *	1981-07-06	1983-01-20	Toyobo Co Ltd	安定な酵素組成物
JPS5865218A (ja) *	1981-10-13	1983-04-18	Kowa Co	組織プラスミノーゲンアクチベーターの製造方法
JPS58107178A (ja) *	1981-12-22	1983-06-25	Mitsui Toatsu Chem Inc	ベ−タ−ガラクトシダ−ゼ又はその複合体の安定な凍結乾燥品
JPS58134991A (ja) *	1981-12-28	1983-08-11	Takeda Chem Ind Ltd	セラチオペプチタ−ゼの安定化法
CA1226795A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized coagulation control products
CA1226794A (en) *	1983-06-06	1987-09-15	Michael K. Hoskins	Stabilized multiparameter control product
US4663295A (en) *	1983-06-29	1987-05-05	Ciba Corning Diagnostics Corp.	Estrogen-progesterone control reagents and methods for making same

1984
- 1984-05-02 CA CA000453361A patent/CA1230300A/en not_active Expired
- 1984-06-04 DK DK275184A patent/DK275184A/da not_active Application Discontinuation
- 1984-06-05 AU AU29085/84A patent/AU583474B2/en not_active Ceased
- 1984-06-05 IL IL72030A patent/IL72030A0/xx unknown
- 1984-06-05 NO NO842258A patent/NO842258L/no unknown
- 1984-06-06 JP JP59114690A patent/JP2596911B2/ja not_active Expired - Lifetime

Also Published As

Publication number	Publication date
NO842258L (no)	1984-12-07
IL72030A0 (en)	1984-10-31
AU583474B2 (en)	1989-05-04
JP2596911B2 (ja)	1997-04-02
JPS606192A (ja)	1985-01-12
DK275184A (da)	1984-12-07
AU2908584A (en)	1984-12-13
DK275184D0 (da)	1984-06-04

Legal Events

Date	Code	Title	Description
2004-12-15	MKEX	Expiry

Publication	Publication Date	Title
US4883762A (en)	1989-11-28	Stabilized isoenzyme control products
Hirschhorn et al.	1978	Adenosine deaminase activity in normal tissues and tissues from a child with severe combined immunodeficiency and adenosine deaminase deficiency
Gracy et al.	1970	Structural relations in aldolases purified from rat liver and muscle and Novikoff hepatoma
Jackson	1969	Studies in the enzymology of glutathione metabolism in human erythrocytes
Soliman et al.	1971	Factors affecting freezing damage of lactic dehydrogenase
Jianguo et al.	1994	Purification and properties of uricase from Candida sp. and its application in uric acid analysis in serum
Heinz et al.	1982	[52] Glyceraldehyde-3-phosphate dehydrogenase from human tissues
McFADDEN et al.	1975	Composition, Quaternary Structure, and Catalytic Properties of d‐Ribulose‐1, 5‐Bisphosphate Carboxylase from Euglena gracilis
US4684615A (en)	1987-08-04	Stabilized isoenzyme control products
MORIMOTO et al.	1970	A release of renin from dog kidney cortex slices
CA1230300A (en)	1987-12-15	Stabilized isoenzyme control product
Hatfield et al.	1970	Threonine Deaminase from Bacillus subtilis: I. PURIFICATION OF THE ENZYME
Rosenberg et al.	1975	The quantitation of rat serum esterases by densitometry of acrylamide gels stained for enzyme activity
Marangos et al.	1974	Multiple Forms of Flounder Muscle Glyceraldehyde 3-Phosphate Dehydrogenase: SUBUNIT COMPOSITION, PROPERTIES, AND TISSUE DISTRIBUTION OF THE FORMS
CN113528609B (zh)	2024-11-01	谷胱甘肽还原酶检测试剂盒及其制备方法和应用
Valentine	1979	The Stratton lecture: hemolytic anemia and inborn errors of metabolism
Gore et al.	1950	The cozymase of mammalian brain
EP0130708A1 (en)	1985-01-09	Stabilized clinical control reagents
Kloosterboer et al.	1976	The development of creatine kinase in rat skeletal muscle. Changes in isoenzyme ratio, protein, RNA and DNA during development
Bergmeyer et al.	2012	Lactate dehydrogenase, isoenzymes
Snead et al.	1978	d-Ribulose-1, 5-biphosphate carboxylase from Thiobacillus neapolitanus
Hjelm et al.	1980	A phosphoglycerate kinase variant, PGK Uppsala, associated with hemolytic anemia
Lee et al.	1973	Electrophoretic variation in glutamate dehydrogenase and other isozymes in wild carrot cells cultured in the presence and absence of 2, 4-dichlorophenoxyacetic acid
US4276376A (en)	1981-06-30	Creatine kinase control serum
Chang et al.	1984	Induction of delta-aminolevulinic acid dehydratase in mouse Friend virus-transformed erythroleukemia cells during erythroid differentiation