Purification and Characterization of a Lecithin-d(-)-β-Hydroxybutyrate Dehydrogenase Complex
Year: 1973
Type: article
Abstract: A complex between partially purified d(-)-β-hydroxybutyrate dehydrogenase from beef heart mitochondria and soybean lecithin was purified. The active complex contains a single type of polypeptide chain of molecular weight 32,000 as determined by sodium dodecyl sulfate-acrylamide gel electrophoresis. The amino acid composition of the polypeptide chain is similar to that of many soluble enzymes, despite the very strong interaction with lecithin vesicles which was demonstrated. Cross-linking experiments with dimethyl suberimidate dihydrochloride failed to disclose any polypeptide aggregates in the enzyme-lecithin complex. The apparent Michaelis constants for all four substrates and the temperature dependence of the initial velocity were determined for the purified complex.
Source: Journal of Biological Chemistry
Authors: Heinrich M. Menzel, Gordon G. Hammes
Institution: Cornell University
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1507499460