Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.

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Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme.

P2860

Q43059801-D75EE1EC-2ECB-470D-BD1B-4AD123E058B0

P2860

Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.

Item

http://www.wikidata.org/entity/Q39681677

description

1979 nî lūn-bûn

@nan

1979年の論文

@ja

1979年論文

@yue

1979年論文

@zh-hant

1979年論文

@zh-hk

1979年論文

@zh-mo

1979年論文

@zh-tw

1979年论文

@wuu

1979年论文

@zh

1979年论文

@zh-cn

name

Purification of alcohol dehydr ...... igand affinity chromatography.

@en

Purification of alcohol dehydr ...... igand affinity chromatography.

@nl

type

Item

label

Purification of alcohol dehydr ...... igand affinity chromatography.

@en

Purification of alcohol dehydr ...... igand affinity chromatography.

@nl

prefLabel

Purification of alcohol dehydr ...... igand affinity chromatography.

@en

Purification of alcohol dehydr ...... igand affinity chromatography.

@nl

P1476

Purification of alcohol dehydr ...... igand affinity chromatography.

@en

P2093

Brown AJ

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

Lee CY

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

P2860

Protein measurement with the Folin phenol reagent

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Double-ternary complex affinity chromatography: preparation of alcohol dehydrogenases

Affinity chromatography of macromolecules.

Purification of kinases by general ligand affinity chromatography.

Alcohol dehydrogenase from Drosophila melanogaster.

Enzyme instability and proteolysis during the purification of an alcohol dehydrogenase from Drosophila melanogaster.

Preparative purification of homogenous steroid-active isozyme of horse liver alcohol dehydrogenase by affinity chromatography on an immobilized AMP-analog.

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

Analysis of bacteriophage T7 early RNAs and proteins on slab gels.

P304

479-482

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scholarly article

P356

10.1042/BJ1790479

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P407

English

P433

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

P478

179

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

P577

1979-06-01T00:00:00Z

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

P5875

23022015

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P698

112998

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P921

Drosophila

P932

1186653

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

Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.

about

P2860

P2860

Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932