PREPARATION AND PROPERTIES OF 2 NEW CHROMOGENIC SUBSTRATES OF TRYPSIN
PREPARATION AND PROPERTIES OF 2 NEW CHROMOGENIC SUBSTRATES OF TRYPSIN
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DOI：
10.1016/0003-9861(61)90145-x
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发表时间：
1961-01-01
影响因子：
3.9
通讯作者：
KOKOWSKY, N
中科院分区：
文献类型：
--
作者：
ERLANGER, BF;COHEN, W;KOKOWSKY, N
本文介绍了L-赖氨酸对硝基苯胺二氢溴酸盐和苯甲酰-DL-精氨酸对硝基苯胺盐酸盐的合成及性质。这两种化合物均被胰蛋白酶水解，后者水解速度快于苯甲酰基L-精氨酸-酰胺。由于产物之一对硝基苯胺是黄色的，因此它们的水解可以方便地用比色法进行。他们与胰蛋白酶反应的Km和K3值进行了测定，以及Ki的苯甲酰基D-精氨酸对硝基苯胺，这是从DL异构体的胰蛋白酶消化分离。还测定了pH-活性曲线，L-LPA的pH-活性曲线比胰蛋白酶底物的pH-活性曲线处于更碱性的区域。这种转变的可能意义进行了讨论。初步研究表明，苯甲酰DL-精氨酸对硝基苯胺盐酸盐也被木瓜蛋白酶水解。
The synthesis and properties of L-lysine p-nitroanilide dihydrobromide and benzoyl DL-arginine p-nitroanilide hydrochloride are described. Both compounds are hydro-lyzed by trypsin, the latter being hydrolyzed faster than benzoyl L-argin-inamide. Their hydrolysis can be followed conveniently by colorimetric procedures, since one of the products, p-nitroaniline, is yellow. Values of Km and k3 for their reaction with trypsin were determined, as well as the Ki of benzoyl D-arginine p-nitroanilide, which was isolated from a tryptic digest of the DL isomer. The pH-activity curves were also determined, that of L-LPA being in a more alkaline region than normally found for trypsin substrates. The possible significance of this shift is discussed. Preliminary studies indicate that benzoyl DL-arginine p-nitroanilide hydrochloride is also hydrolyzed by papain.