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Purification and properties of human serum dopamine-beta-hydroxylase.

作者信息

Ikeno T, Hashimoto S, Kuzuya H, Nagatsu T

出版信息

Mol Cell Biochem. 1977 Dec 29;18(2-3):117-23. doi: 10.1007/BF00280277.

Abstract
  1. Two different molecular forms of dopamine-beta-hydroxylase were isolated from human serum; a major component (Peak I enzyme) with a molecular weight of 368000 and with a higher specific activity and a minor component (Peak II enzyme) with a molecular weight of 188000 and with a lower specific activity. 2. Both forms require ascorbic acid for the activity, and are stimulated by fumarate. Addition of N-ethylmaleimide or copper also increased the activity. The optimal pH of both forms in the presence of 20mM tyramine as substrate is 5.0. 3. Km values toward tyramine of Peak I enzyme and Peak II enzyme were 1.67 mM and 14.2 mM respectively. 4. Both Peak I enzyme and Peak II enzyme are glycoprotein.
摘要

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