MECHANISM OF INHIBITION OF PEPSIN BY PEPSTATIN. II
SETSUKO KUNIMOTO, TAKAAKI AOYAGI, RINZO NISHIZAWA, TOMOYOSHI KOMAI, TOMIO TAKEUCHI, HAMAO UMEZAWA
著者情報
1974 年 27 巻 6 号 p. 413-418
詳細
1974 年 27 巻 6 号 p. 413-418
Pepstatin, a strongly bound inhibitor of acid proteases, does not instantaneously bind to pepsin. The dissociation constant of pepsin-pepstatin complex is 9.7 × 10-11 M using Phe•Gly•His•Phe(NO2)•Phe•Ala•PheOMe as substrate. Difference ultraviolet absorption spectra show conformational change of pepsin in interaction with pepstatin. The bindillg of pepsin with pepstatin is stoicheometric and the normality of pepsin can be easily titrated by pepstain. Pepsin modified by 1, 2-epoxy-3-(p-nitrophenoxy) propane, 2, 3-butanedione, α-diazo-p-bromoacetophenone or p-bromophenacyl bromide shows reduced pepstatin-binding activity.
