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The binding by an NAD-affinity matrix of contaminating dehydrogenases in cytochrome c oxidase preparations.

作者信息

Holbrook J, Bucher J, Penniall R

出版信息

Hoppe Seylers Z Physiol Chem. 1976 May;357(5):623-7. doi: 10.1515/bchm2.1976.357.1.623.

Abstract

An NAD-matrix is capable of the separation of three contaminant reductase activities from highly purified beef heart cytochrome c oxidase. Non-specific binding of cytochrome c oxidase occurs as well. When the matrix is saturated with respect to the non-specific binding, continued binding of the reductases can be observed. As a consequence of equilibration with the matrix, the turnover numbers of the unbound cytochrome c oxidase are increased.

摘要

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