KINETICS OF THE REACTION OF RENIN WITH NINE SYNTHETIC PEPTIDE SUBSTRATES

摘要: A number of peptides have been synthesized which represent portions the tetradecapeptide renin substrate molecule, and contain hydrolyzable leu-leu bond. An automatic chemical method for determination velocity reaction with these compounds was developed. Application at several levels concentration permitted construction Lineweaver-Burk plots, calculation Michaelis constants (Km) maximal velocities (Vmax). The results show that maximum affinity enzyme (lowest Km) is achieved only full molecule (asp1-arg2-val3-tyr4-ileu5-his6-pro7-phe8-his9-leu10-leu11-val12-tyr13-ser14). Removal asp1 arg2 from N-terminal increases Km eight-fold. Further, moderate increase in occurs when next amino acids, val3, tyr4 ileu5, are removed. further removal his6 a marked reduction Vmax. ser14 C-terminal nonapeptide his6-pro7-phe8-his9-leu10-leu11-val12-tyr13-ser14 does not greatly affect nor Further tyr13 this compound complete loss activity. It suggested or his6-pro7-phe8-his9-leu10-leu11-val12-tyr13 might be used as substrates assay standardization renin.