Elsevier

Biochemical Pharmacology

Volume 35, Issue 24, 15 December 1986, Pages 4499-4503
Biochemical Pharmacology

Hydrolysis of neo-kyotorphin (Thr-Ser-Lys-Tyr-Arg) and [Met]enkephalin-Arg6-Phe7 by angiotensin-converting enzyme from monkey brain

https://doi.org/10.1016/0006-2952(86)90770-7Get rights and content

Abstract

Angiotensin-converting enzyme (ACE; dipeptidyl carboxypeptidase, EC 3.4.15.1) from monkey brain was partially purified 274-fold with 4.5% yield. The optimum pH of the enzyme was 8.2, and its Km was 3.3 mM, with hippuryl-His-Leu as the substrate in 300 mM NaCl. Its molecular weight (Mr) was estimated to approximately 260,000 by gel filtration on Sephadex G-200. On high-performance liquid chromatographic analysis, ACE hydrolyzed neo-kyotorphin (Thr-Ser-Lys-Tyr-Arg) with liberation of kyotorphin (Tyr-Arg), the [Met]enkephalin releasor. ACE also converted [Met]enkephalin-Arg6-Phe7 to [Met]enkephalin; then the enzyme slowly hydrolyzed the resulting [Met]enkephalin. The Km values of the enzyme for neo-kyotorphin and [Met]enkephalin-Arg6-Phe7 were 0.58 and 0.30 mM respectively. Thus, brain ACE may have a role in the formation of kyotorphin and [Met]enkephalin from their precursors but has little part in [Met]enkephalin degrading process.

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