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https://open.uns.ac.rs/handle/123456789/14588
Title: | Coenzyme binding capacity of yeast alcohol dehydrogenase | Authors: | Leskovac V. Peričin D. |
Issue Date: | 30-Mar-1978 | Journal: | Biochemical and Biophysical Research Communications | Abstract: | Commercial lyophilized preparations of yeast alcohol dehydrogenase from Boehringer G.m.b.H. (Mannheim, Germany) bind 2 mols of reduced coenzyme/144000 g of enzyme (1). After the purification by a DEAE-Sephadex column chromatography, the coenzyme binding capacity is raised to 4 mols of NADH/mol of enzyme. Commercial preparations and ionexchange-purified preparations are homogeneous on the ionexchange column chromatography and the disc gel electrophoresis, after reduction with thioglycolic acid. Ionexchange chromatography does not increase the -SH titer, zinc content and the specific activity of enzyme. It is suggested that ionexchange chromatography raises the NADH-binding capacity by removing some impurities present in commercial enzyme preparations. © 1978. | URI: | https://open.uns.ac.rs/handle/123456789/14588 | ISSN: | 0006291X | DOI: | 10.1016/0006-291X(78)91550-4 |
Appears in Collections: | TF Publikacije/Publications |
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