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Lipoamide dehyrogenase immobilized on porous glass.

作者信息

Scouten W H, Knowles H, Freitag L C, Iobst W

出版信息

Biochim Biophys Acta. 1977 May 12;482(1):11-8. doi: 10.1016/0005-2744(77)90348-5.

Abstract

Lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) isolate from pig heart and Escherichia coli was covalently coupled by both diazonium and amide bonds to controlled pore glass beads (96% silica). When the enzyme was immobilized in the presence of NAD+, the enzyme no longer exhibited its normal requirement for NAD+ for full activity. If the immobilized enzyme was then treated with NADase, the requirement for NAD+ was restored. Enzyme immobilized in the absence of NAD+ exhibited normal NAD+ dependence both prior to an after NADase treatment. These results are discussed in terms of co-immobilization of NAD+ at or near the allosteric site of the enzyme.

摘要

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