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

Search MEDLINE/PubMed


  • Title: Separation of carboxypeptidase A and B from longitudinal muscle layer of bovine small intestine: their properties regarding hydrolysis of enkephalins and enkephalin-analogs.
    Author: Kase R, Hideshima C, Hazato T.
    Journal: Biochem Int; 1987 May; 14(5):889-96. PubMed ID: 3454645.
    Abstract:
    Carboxypeptidase A and B were partially purified from the soluble fraction of longitudinal muscle layer (myenteric plexus) of bovine small intestine. The obtained carboxypeptidase A hydrolyzed [Met]enkephalin-Arg6-Phe7 and [Leu]enkephalin, but [Met]enkephalin was not a suitable substrate for the enzyme. The Km value of carboxypeptidase A for [Met]enkephalin-Arg6-Phe7 was 0.74 mM and that for [Leu]enkephalin was 0.44 mM. Intestinal carboxypeptidase B hydrolyzed [Met]enkephalin-Arg6, liberating [Met]enkephalin, and the Km value of the enzyme for [Met]enkephalin-Arg6 was 0347 mM.
    [Abstract] [Full Text] [Related] [New Search]