Characterization of a membrane-associated NADH-dependent cytochrome C reductase of human platelets
| Autor: | David P. Kosow, Gary Moroff |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Blood Platelets
Time Factors Platelet Aggregation Cytochrome Cytochrome c Group Reductase Superoxide dismutase chemistry.chemical_compound Tetracaine Humans Cytochrome Reductases chemistry.chemical_classification biology Superoxide Cytochrome c Cell Membrane Cytochrome P450 reductase NADH Dehydrogenase Hematology Enzyme chemistry Biochemistry Quinacrine biology.protein Platelet aggregation inhibitor Chloromercuribenzoates |
| Zdroj: | Thrombosis Research. 23:23-31 |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/0049-3848(81)90234-6 |
| Popis: | Platelet membranes isolated by the glycerol lysis technique contain a NADH-dependent reductase which reduces cytochrome c. The K NADH of the membrane associated enzyme was 1.3 μM and the Vmax of the reaction was 4600 nmoles cytochrome c reduced/min/mg protein. Superoxide dismutase had no affect on the reaction indicating that reduction was independent of superoxide formation. The reductase was inhibited by the drugs quinacrine HC1, quercetin and tetracaine HC1 and also by PCMBS(p-chloromercuribenzoate sulfonate). Aggregation in citrated plasma induced by ADP, collagen and the ionophore A23187 were also inhibited by quinacrine HC1, quercetin and tetracaine HC1. It is possible that the inhibition of both the reductase activity and aggregation by these compounds reflects a role for the membrane-associated reductase in one of the processes which leads to the aggregation of platelets. |
| Databáze: | OpenAIRE |
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