Literature DB >> 112998

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

A J Brown, C Y Lee.   

Abstract

A method for the purification of alcohol dehydrogenase from Drosophila melanogaster is described. The method makes use of 8-(6-aminohexyl)amino-5'-AMP, immobilized on Sepharose 4B, as an affinity ligand. Since alcohol dehydrogenase from Drosophila shows weak affinity for this column, a novel technique was developed to separate alcohol dehydrogenase from both unbound proteins and more strongly bound enzymes. The purification procedure is simple to operate and give a homogeneous preparation in good yield after only three steps.

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Year:  1979        PMID： 112998      PMCID： PMC1186653          DOI： 10.1042/bj1790479

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  17 in total

1.  LIVER ALCOHOL DEHYDROGENASE-DPN-PYRAZOLE COMPLEX: A MODEL OF A TERNARY INTERMEDIATE IN THE ENZYME REACTION.

Authors:  H THEORELL; T YONETANI
Journal:  Biochem Z       Date:  1963

2.  GENETIC VARIATION OF ALCOHOL DEHYDROGENASE IN DROSOPHILIA MELANOGASTER.

Authors:  F M JOHNSON; C DENNISTON
Journal:  Nature       Date:  1964-11-28       Impact factor: 49.962

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

Authors:  L Anderson; H Jornvall; K Mosbach
Journal:  Anal Biochem       Date:  1975-12       Impact factor: 3.365

4.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

5.  Alcohol dehydrogenase from Drosophila melanogaster.

Authors:  J I Elliott; J A Knopp
Journal:  Methods Enzymol       Date:  1975       Impact factor: 1.600

6.  Purification of kinases by general ligand affinity chromatography.

Authors:  C Y Lee; L H Lazarus; D S Kabakoff; P J Russell; M Laver; N O Kaplan
Journal:  Arch Biochem Biophys       Date:  1977-01-15       Impact factor: 4.013

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

Authors:  D R Thatcher
Journal:  Biochem J       Date:  1977-05-01       Impact factor: 3.857

8.  Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster.

Authors:  T H Day; P C Hillier; B Clarke
Journal:  Biochem Genet       Date:  1974-02       Impact factor: 1.890

9.  Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster.

Authors:  C L Vigue; F M Johnson
Journal:  Biochem Genet       Date:  1973-07       Impact factor: 1.890

10.  Alcohol dehydrogenase of Drosophila: interconversion of isoenzymes.

Authors:  K B Jacobson
Journal:  Science       Date:  1968-01-19       Impact factor: 47.728
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  3 in total

1.  Co-purification of coenzyme-dependent enzymes by affinity chromatography.

Authors:  C Y Lee
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396

2.  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.

Authors:  E Juan; R González-Duarte
Journal:  Biochem J       Date:  1981-04-01       Impact factor: 3.857

3.  Drosophila lactate dehydrogenase: molecular and genetic aspects.

Authors:  A Onoufriou; S N Alahiotis
Journal:  Biochem Genet       Date:  1982-12       Impact factor: 1.890
  3 in total

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