| Literature DB >> 213050 |
A H Kolk, L van Kuyk, B Boettcher.
Abstract
Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the other isoenzymes. The purified human isoenzyme LDH-X had a specific activity of 146 units/mg of protein.Entities:
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Year: 1978 PMID: 213050 PMCID: PMC1185842 DOI: 10.1042/bj1730767
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857