PEPTIDASES IN MAMMALIAN PLATELETS. II. THE HYDROLYSIS OF L-LEUCYLGLYCINE AND OF OTHER DIAND TRIPEPTIDES BY HUMAN PLATELETS
Abstract
THE HYDROLYSIS OF L-LEUCYLGLYCINE BY NORMAL HUMAN PLATELETS PROCEEDS OPTIMALLY AT PH 8.4 IN PHOSPHATE BUFFER AND IS ENHANCED BY THE ADDITITION OF ZN++. OTHER DIPEPTIDES LIKE GLYCYL-L-TYROSINE, L-ALANYLGLYCINE AND GLYCYL-L-ALANINE ARE HYDROLYZED AT A FASTER RATE IN THE ABSENCE OF CO++ THAN IN ITS PRESENCE. PLATELETS ALSO CONTAIN A PROLINASE AS DEMONSTRATED BY THE HYDROLYSIS OF PROLYL-GLYCINE. TRIPEPTIDASE ACTIVITY, MEASURED WITH BLYCYLGLYCYLGLYCINE AS SUBSTRATE SHOWED A PH OPTIMUM AT 7.4. VARIOUS OTHER TRIPEPTIDES ARE ALSO HYDROLYZED
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 14, 1960
- Accession Number
- AD0248882
Entities
People
- W. Kocholaty
Organizations
- United States Army Medical Research Laboratory