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Biochem J ; 227(2): 467-74, 1985 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-4004775

RESUMO

The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions.


Assuntos
Reagentes de Ligações Cruzadas , Redutases do Citocromo , Mitocôndrias Cardíacas/enzimologia , NADH Desidrogenase , Animais , Sítios de Ligação , Bovinos , Redutases do Citocromo/imunologia , Eletroforese em Gel de Poliacrilamida , Metaloproteínas/análise , NAD , NADH Desidrogenase/imunologia , Succinimidas
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