These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Hydrolysis of neo-kyotorphin (Thr-Ser-Lys-Tyr-Arg) and [Met]enkephalin-Arg6-Phe7 by angiotensin-converting enzyme from monkey brain.
    Author: Kase R, Sekine R, Katayama T, Takagi H, Hazato T.
    Journal: Biochem Pharmacol; 1986 Dec 15; 35(24):4499-503. PubMed ID: 3024652.
    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 be 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 releaser. 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 processes.
    [Abstract] [Full Text] [Related] [New Search]