ACIDIC TRANSITION OF DELTA-CHYMOTRYPSIN
ACIDIC TRANSITION OF DELTA-CHYMOTRYPSIN
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DOI：
10.1021/bi00712a018
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发表时间：
1974-01-01
期刊：
影响因子：
2.9
通讯作者：
LABOUESSE, B
中科院分区：
文献类型：
--
作者：
GAREL, JR;EPELY, S;LABOUESSE, B
胰凝乳蛋白酶原和<$-胰凝乳蛋白酶的行为已研究在酸性pH值的旋光度，吸收，和荧光测量;这两种蛋白质显示pH依赖性的变化。动力学实验使用吸收或荧光和pH跃变方法证明了一个缓慢的过程，发生在酶中，而不是在其酶原中;这个缓慢的过程是由一个基团的电离控制的，PA”为3，并涉及大的荧光变化。通过从酶原中观察到的变化中校正等离子时在胰凝乳蛋白酶中观察到的变化，人们可以评估与基团电离特异性相关的变化。
The behaviors of chymotrypsinogenand¿-chymotrypsin have been studied at acidic pH by optical rotation, ab-sorption, and fluorescence measurements; both proteins show pH-dependent changes. Kinetic experiments using either absorption or fluorescence and a pH jump method have evidenced a slow process which takes place in the enzyme and not in its zymogen; this slow process is controlled by the ionization of a group with a pA" of 3, and involveslarge fluorescence changes. By correcting the changes observed in¿-chymotrypsin at equi-librium from those observed in the zymogen, one may evaluate the variations specifically linked to the ionizationof the group