doi: 10.1042/bj1790479.
Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography
- PMID: 112998
- PMCID: PMC1186653
- DOI: 10.1042/bj1790479
Item in Clipboard
Purification of alcohol dehydrogenase from Drosophila by general-ligand affinity chromatography
Biochem J.
.
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.
Similar articles
-
Purification and enzyme stability of alcohol dehydrogenase from Drosophila simulans, Drosophila virilis and Drosophila melanogaster adhS.Biochem J. 1980 Jul 1;189(1):105-10. doi: 10.1042/bj1890105. Biochem J. 1980. PMID: 6779810 Free PMC article.
-
Purification and separation of pyridine nucleotide-linked dehydrogenases by affinity chromatography techniques.Proc Natl Acad Sci U S A. 1974 Sep;71(9):3450-4. doi: 10.1073/pnas.71.9.3450. Proc Natl Acad Sci U S A. 1974. PMID: 4372619 Free PMC article.
-
Separation of isozymes of horse liver alcohol dehydrogenase and purification of the enzyme by affinity chromatography on an immobilized AMP-analogue.Biochim Biophys Acta. 1974 Sep 11;364(1):1-8. doi: 10.1016/0005-2744(74)90126-0. Biochim Biophys Acta. 1974. PMID: 4373066 No abstract available.
-
The synthesis of three AMP-analogues: N6-(6-aminohexyl)-adenosine 5'-monophosphate, N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate, and N6-(6-aminohexyl)-adenosine 3',5'-bisphosphate and their application as general ligands in biospecific affinity chromatography.Eur J Biochem. 1974 Aug 15;47(1):81-9. doi: 10.1111/j.1432-1033.1974.tb03670.x. Eur J Biochem. 1974. PMID: 4474079 No abstract available.
-
Enzyme instability and proteolysis during the purification of an alcohol dehydrogenase from Drosophila melanogaster.Biochem J. 1977 May 1;163(2):317-23. doi: 10.1042/bj1630317. Biochem J. 1977. PMID: 405973 Free PMC article.
Cited by
-
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.Biochem J. 1981 Apr 1;195(1):61-9. doi: 10.1042/bj1950061. Biochem J. 1981. PMID: 6796069 Free PMC article.
-
Drosophila lactate dehydrogenase: molecular and genetic aspects.Biochem Genet. 1982 Dec;20(11-12):1195-1209. doi: 10.1007/BF00498943. Biochem Genet. 1982. PMID: 6819859
-
Co-purification of coenzyme-dependent enzymes by affinity chromatography.Mol Cell Biochem. 1983;57(1):27-40. doi: 10.1007/BF00223522. Mol Cell Biochem. 1983. PMID: 6646117
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
