Tissue specific isoenzymes of d-lactate dehydrogenase from the foot,mantle and hepatopancreas of Patella caerulea (L). purification and properties |
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Institution: | 1. Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA;2. State Key Laboratory of Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, Sichuan 610041, PR China |
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Abstract: | - 1.1. Isoenzymes of d-lactate specific dehydrogenase from foot, mantle and hepatopancreas of Patella caerulea have been purified by Chromatographic techniques. d-lactate dehydrogenase (d-Ldh) from P. caerulea tissues was found to be tetrameric with a Mr of ca 140,000 as judged by gel filtration; subunit Mr of ca 37,000 was obtained from SDS-electrophoresis.
- 2.2. Kinetic studies suggest that P. caerulea foot and mantle d-Ldh is similar to vertebrate muscle-type l-Ldh; furthermore hepatopancreas d-LDH resembles vertebrate heart-type l-LDH since it has a higher affinity for d-lactate and is inhibited by pyruvate.
- 3.3. The results imply that the P. caerulead-Ldh isoenzymes may have distinct metabolic functions.
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