| Literature DB >> 7213742 |
M A Coletti-Previero, H Mattras, B Descomps, A Previero.
Abstract
A 5000-fold purification of the enzyme responsible for the rapid inactivation of enkephalin in human blood has been achieved: this enzyme cleaves the N-terminal tyrosine from enkephalin and from short peptides provided their first amino acid is aromatic. The enzyme, an enkephalin-degrading aminopeptidase (alpha-aminoacyl-peptide hydrolase, EC 3.4.11.11), requires a free amino group on the substrate and has a maximum activity around pH 8. Its appearance molecular weight is in the range of 80 000-90 000 and an apparent Michaelis constant of 0.4 mM was determined.Entities:
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Year: 1981 PMID： 7213742 DOI： 10.1016/0005-2744(81)90135-2
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002