Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism - Wikidata - awgldk - TriplyDB

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

http://www.wikidata.org/entity/Q41942761

about

Kinetics of carbonyl reductase from human brain Cataract development in diabetic sand rats treated with alpha-lipoic acid and its gamma-linolenic acid conjugate.From metabolomics to fluxomics: a computational procedure to translate metabolite profiles into metabolic fluxes Aldose reductase inhibitors and cataract.Medicinal chemistry of aldose reductase inhibitors.Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells.Low apparent aldose reductase activity produced by monosaccharide autoxidation.Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3 alpha-hydroxysteroid dehydrogenase.Kinetic studies with the low-Km aldehyde reductase from ox brain Rat lens aldose reductase and polyol production.In vivo pharmacokinetics of aldose reductase inhibitors: 3-fluoro-3-deoxy-D-glucose NMR studies in rat brains.Noninvasive analysis of aldose reductase activities in rat testis: 3-FDG NMR spectroscopy and imaging.Effects of long-acting somatostatin analogues on redox systems in rat lens in experimental diabetes.Simple graphical methods for use with complex ligand-binding and enzyme mechanisms.Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification.

P2860

Q24529495-CF6A8486-336F-4D68-A54D-E360DFBF6A63 Q32164813-2682A031-6712-422C-8928-8BD385E054BB Q34456888-722800A9-03E6-44BF-9997-3E6BAEBE5B31 Q37326897-C4BB8F2E-B1E4-4904-8AF8-D1D9448E0C5C Q39603319-12435037-B115-4240-A4E0-D2A700824CFB Q40919255-5E841B02-2F7C-4E56-B1DA-AD2214D61A98 Q42095060-C0B9843C-6973-4C91-832B-293AEE17A7FB Q42830552-11F664E5-A140-499D-B67D-DD63D5C8B90F Q42849493-6F564289-6C81-4A9C-BD62-5A8D29CE6B89 Q42857024-4FD1661E-6E5F-41C2-A056-C937290D6BBB Q46120139-229EC859-3F43-4071-A026-B9ED3A11BE71 Q46512523-D9A399B9-E748-4680-91B6-435AD429407E Q50682395-0C1C7335-4E07-4918-AC6D-85D56DC1647A Q52559016-872348CE-BEE9-4AA4-9445-55FA5693EF8E Q54371888-4B8B773E-9FA5-493C-9780-A53BCEBF1732

P2860

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

http://www.wikidata.org/entity/Q41942761

description

1984 nî lūn-bûn

@nan

1984年の論文

@ja

1984年論文

@yue

1984年論文

@zh-hant

1984年論文

@zh-hk

1984年論文

@zh-mo

1984年論文

@zh-tw

1984年论文

@wuu

1984年论文

@zh

1984年论文

@zh-cn

name

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

@en

type

label

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

@en

prefLabel

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

@en

P1433

Q41942761-51D9D70B-671B-48B5-A821-EAB012944D80

P1476

Q41942761-216F2656-4E13-4BFE-B9FB-19CC0AC7DBCE

P2093

Q41942761-1F4AABF0-D786-4719-999A-E5620F82BF71

Q41942761-3BB570D4-10C5-46D6-8109-A02C17826BD4

P2860

Q41942761-0A8C7390-5957-4955-96B6-C60A3115434B

Q41942761-2C2BE661-939C-423D-9AA6-0DBC954C39CA

Q41942761-4C759C83-BC28-4843-8B3D-74F1E6168456

Q41942761-63B88738-302C-4A13-AE29-1D23F68CD283

Q41942761-7991D80E-4ED3-454C-8FC6-F9D35AA50715

Q41942761-AA16DC64-0025-4CD2-87D0-77CFD5538053

Q41942761-AF2D096A-AC51-4791-8589-9D7A870B0A54

Q41942761-EF8D6B97-C8AE-418B-8FE2-9B9BF033B51B

P304

Q41942761-76A9463C-0AA0-464A-A9A6-FAFC9828979E

P31

Q41942761-E0E36034-6082-4DBF-94F6-3F8BCAE3FB51

P356

Q41942761-A4B4EDB5-61E8-430A-89C5-80CF6A7C80B6

P407

Q41942761-E5A559F8-502F-4855-B4BA-63EDB82A63D8

P433

Q41942761-F0A53FCE-DD2C-46B0-BDD1-D0BE1E9CCB70

P478

Q41942761-E962DD4A-039D-4C95-8B7D-47EDCE35E02E

P577

Q41942761-5F46FCEF-FC34-482B-AE31-87CC71C98F18

P5875

Q41942761-BA50F41A-8B6B-4552-AD90-9306917BDC99

P698

Q41942761-836200F4-DC86-4EAB-858A-1A93B36ACF08

P932

Q41942761-F6C559A4-6328-4BF5-8CB4-515C131CC959

P356

P1433

Biochemical Journal

P1476

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism

@en

P2093

Crabbe MJ

http://www.w3.org/2001/XMLSchema#string

Halder AB

http://www.w3.org/2001/XMLSchema#string

P2860

Protein measurement with the Folin phenol reagent

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The sorbitol pathway in the human lens: aldose reductase and polyol dehydrogenase.

Physical and kinetic properties of homogenous bovine lens aldose reductase.

The oxidation of oxyhaemoglobin by glyceraldehyde and other simple monosaccharides.

Bovine lens aldehyde dehydrogenase. Purification and preliminary characterization.

Purification and characterization of an enzymically active cleavage product of pig kidney aldehyde reductase.

General ligands in affinity chromatography. Cofactor-substrate elution of enzymes bound to the immobilized nucleotides adenosine 5'-monophosphate and nicotinamide-adenine dinucleotide.

P304

33-39

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1042/BJ2190033

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

219

http://www.w3.org/2001/XMLSchema#string

P577

1984-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

16768776

http://www.w3.org/2001/XMLSchema#string

P698

6426471

http://www.w3.org/2001/XMLSchema#string

P932

1153445

http://www.w3.org/2001/XMLSchema#string