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- W2894328867 abstract "Abstract Human liver alcohol dehydrogenase (ADH, EC 1.1.1.1) is a large and heterogeneous family of isoenzymes and the high-performance liquid chromatographic peptide mapping technique which was developed here recognizes differences and similarities between them. Isoenzymes were S -carboxymethylated, digested with trypsin, and the mixtures of tryptic peptides fractionated by reverse-phase gradient chromatography on octadecylsilane columns, using perchlorate-phosphate buffer and acetonitrile as eluants. The resultant peptide maps were reproducible, showing great similarities between the αβγ-ADH isoenzymes (now called Class I) on the one hand and remarkable differences between these and both the π- and χ-ADH isoenzymes (now called Class II and III, respectively) on the other. This implies that these three isoenzyme groups have characteristic primary structures which correspond to their typical substrate specificities and kinetics." @default.
- W2894328867 created "2018-10-05" @default.
- W2894328867 creator A5020132888 @default.
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- W2894328867 date "1983-01-01" @default.
- W2894328867 modified "2023-09-27" @default.
- W2894328867 title "Characterization of Human Alcohol Dehydrogenase Isoenzymes by High-Performance Liquid Chromatographic Peptide Mapping**This paper was presented at the International Symposium on HPLC of Proteins and Peptides, November 16–17, 1981, Washington, D. C." @default.
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- W2894328867 doi "https://doi.org/10.1016/b978-0-12-335780-9.50011-5" @default.
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