A comparison of the structural and functional properties of cytochrome c oxidase isolated from beef (Bos tauros), camel (Camelus dromedarius), chicken (Gallus domesticus) and rat (Rattus norvegicus)-Reference-Cited by-同舟云学术

A comparison of the structural and functional properties of cytochrome c oxidase isolated from beef (Bos tauros), camel (Camelus dromedarius), chicken (Gallus domesticus) and rat (Rattus norvegicus)

Published:1981-01 Issue:3 Volume:68 Page:445-456
ISSN:0305-0491
Container-title:Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
language:en
Short-container-title:Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

Author:

Darley-Usmar V.M.,Alizai N.,Al-Ayash A.I.,Jones G.D.,Sharpe A.,Wilson M.T.

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Physiology,Biochemistry

Reference44 articles.

1. Oxygen “pulsed” cytochrome c oxidase: Functional properties and catalytic relevance;Antonini,1977

2. Binding of arylazidocytochrome c derivatives to beef heart cytochrome c oxidase: cross linking in the high and low affinity binding sites;Bisson;Biochemistry,1980

3. The subunit composition of beef heart cytochrome c oxidase;Bucher;FEBS Lett.,1975

4. Near neighbour relationships of the subunits of cytochrome c oxidase;Briggs;Biochemistry,1977

5. Functional intermediates of cytochrome c oxidase;Brunori;J. biol. Chem.,1979

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