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Properties of water-insoluble matrix-bound lactate dehydrogenase.
Authors:A S Levi
Institution:1. Department of Biochemistry, School of Dental Medicine, Southern Illinois University, Edwardsuille, Illinois 62025 USA;2. Department of Chemistry, University of California, San Diego, La Jolla, California 92037 USA
Abstract:Lactate dehydrogenase enzyme was immobilized by binding to a cyanogen bromideactivated Sepharose 4B-200 in 0.1 m phosphate buffer, pH 8.5. The immobilized enzyme was found to have lower Km values for its substrates. Km values for pyruvate and lactate were 8 × 10 ?5m and 4 × 10?3m, respectively, an order of magnitude less than the value for the native (free) enzyme. Chicken heart (H4) lactate dehydrogenase was found to lose nearly all its substrate inhibition characteristics as a result of immobilization. The covalently bound muscle-type subunits of lactate dehydrogenase showed more favorable interaction with the muscle type than with the heart type subunits. An increase in thermal and acid stability of the dogfish muscle (M4) lactate dehydrogenase as well as a decrease in the percentage of inhibition of enzyme activity by rabbit antisera and in the complement fixation was observed as a result of immobilization. The changes in the properties of the enzyme as a result of immobilization may be attributable to hindrance produced by the insoluble matrix as well as conformational changes in the enzyme molecules.
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