Abstract
Abstract The arginine amidase and arginine esterase activity of human plasma is compared with that of trypsin, thrombin, plasmin, and kallikrein by using the homologous synthetic amino acid substrates, benzoyl arginine amide (BAA) and benzoyl arginine ethyl ester (BAEE). Hydrolyses of BAA and BAEE in plasma are distinguished by several features: pH optimum, heat stability, storage stability, effect of dilution, surface contact activation, streptokinase activation, inhibition by proteolytic enzyme inhibitor, and range of normal variation. The differential sensitivity of trypsin, thrombin, plasmin, and kallikrein toward these substrates and the similarity in reaction characteristics of plasma-BAA and trypsin-BAA provide evidence that the arginine amidase activity of plasma represents trypsin, while the arginine esterase activity of plasma is nonspecific.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
