Rogez D, Cerf R, Andrianjara R, Salehi S T, Fouladgar H
FEBS Lett. 1987 Jul 13;219(1):22-6. doi: 10.1016/0014-5793(87)81183-3.
Ultrasonic relaxation measurements for alpha-chymotrypsin in phosphate, sulfite and arsenate buffers exhibit a high peak of absorption at neutral pH. The analysis is based on: comparison of the relaxation measurements for the enzyme and for the zymogen and inhibited enzyme; X-ray and neutron diffraction data, and high-resolution NMR data. The ultrasonic relaxation is shown to result mainly from a proton-transfer reaction that involves the histidine at the catalytic site (His-57). The question is raised of whether the enhanced ultrasonic effect observed in the enzyme is indicative of a property that plays a part in the catalytic activity.
在磷酸盐、亚硫酸盐和砷酸盐缓冲液中对α-糜蛋白酶进行的超声弛豫测量显示，在中性pH值下有一个高吸收峰。该分析基于：对酶、酶原和抑制酶的弛豫测量结果进行比较；X射线和中子衍射数据，以及高分辨率核磁共振数据。结果表明，超声弛豫主要源于涉及催化位点（His-57）处组氨酸的质子转移反应。由此提出一个问题，即在酶中观察到的增强超声效应是否表明一种在催化活性中起作用的特性。
