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: Kinin-inactivating endopeptidase from rat liver.
    Author: Kouyoumdjian M, Borges DR, Prado JL.
    Journal: Int J Biochem; 1984; 16(7):733-9. PubMed ID: 6381163.
    Abstract:
    A kinin-inactivating serine-endopeptidase from rat liver was purified to an activity of 912 mU/mg of protein, when measured on bradykinin. The endopeptidase molecular weight, estimated by gel filtration, was 68,000. Its isoelectric point was close to pH 4.9. Vm for the hydrolysis of bradykinin, was 1.25 mumol/min/mg protein; Km was 28 microM. The two hydrolysis products from bradykinin were the pentapeptide Arg1-Phe5 and the tetrapeptide Ser6-Arg9.
    [Abstract] [Full Text] [Related] [New Search]