Accession Number:

AD0248882

Title:

PEPTIDASES IN MAMMALIAN PLATELETS. II. THE HYDROLYSIS OF L-LEUCYLGLYCINE AND OF OTHER DIAND TRIPEPTIDES BY HUMAN PLATELETS

Descriptive Note:

Corporate Author:

ARMY MEDICAL RESEARCH LAB FORT KNOX KY

Personal Author(s):

Report Date:

1960-11-14

Pagination or Media Count:

7.0

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

Subject Categories:

Distribution Statement:

APPROVED FOR PUBLIC RELEASE