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Tissue-specific Regulation of Bovine Heart Cytochrome-C Oxidase Activity by ADP via Interaction With Subunit VIa

Tissue-specific Regulation of Bovine Heart Cytochrome-C Oxidase Activity by ADP via Interaction With Subunit VIa

G Anthony, A Reimann, B Kadenbach

Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1652-6.

PMID: 8383320

Abstract:

The activity of reconstituted cytochrome-c oxidase (EC 1.9.3.1) from bovine heart is stimulated by intraliposomal ADP but not by NaCl of the same ionic strength. A monoclonal antibody which reacts with subunits VIa-H (heart-type) and VIc, due to the evolutionary relationship between these subunits, also stimulates the activity of the enzyme from bovine heart but not from bovine liver. The antibody induces a conformational change in the heart enzyme but not in the liver enzyme, as shown by the visible difference spectrum. Preincubation of heart cytochrome-c oxidase with the antibody prevents stimulation of activity by intraliposomal ADP after reconstitution in liposomes. Reconstituted liver cytochrome c oxidase is not stimulated by intraliposomal ADP. The data suggest tissue-specific regulation of the activity of cytochrome-c oxidase by ADP via interaction with the matrix domain of subunit VIa-H.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001165	Cytochrome c Oxidase from bovine heart		9001-16-5	Price

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