Autor: |
Zinov'eva ME, Kaprel'iants AS, Ostrovskiĭ DN |
Jazyk: |
ruština |
Zdroj: |
Biokhimiia (Moscow, Russia) [Biokhimiia] 1983 Aug; Vol. 48 (8), pp. 1319-23. |
Abstrakt: |
A complete cross-linking of proteins in isolated Micrococcus lysodeikticus membranes under effect of glutaric aldehyde causes 50% inhibition of the NADH-oxidase activity. Using the irradiation inactivation procedure, it was demonstrated that the size of the irradiation target for NADH-oxidase coincides with that for NADH-dehydrogenase and makes up to about 50 KD. In glutaric aldehyde-treated membranes the target size for NADH-oxidase is 3 times more than that, i.e. 150 KD. It is assumed that the effective electron transfer is mediated by a carrier assembly united into a supramolecular complex with a terminal life-time. Different assemblies exchange their components due to lateral diffusion of proteins in the membrane, which can account for the small size of the irradiation target for the oxidase activity. |
Databáze: |
MEDLINE |
Externí odkaz: |
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