A KALLIKREIN-LIKE SERINE PROTEASE IN PROSTATIC FLUID CLEAVES THE PREDOMINANT SEMINAL-VESICLE PROTEIN
A KALLIKREIN-LIKE SERINE PROTEASE IN PROSTATIC FLUID CLEAVES THE PREDOMINANT SEMINAL-VESICLE PROTEIN
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DOI：
10.1172/jci112185
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发表时间：
1985-01-01
影响因子：
15.9
通讯作者：
LILJA, H
中科院分区：
文献类型：
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作者：
LILJA, H
从人精浆中纯化出同质的 33 kD 糖蛋白，称为“前列腺特异性抗原”。该前列腺蛋白被鉴定为丝氨酸蛋白酶，其 NH2 末端序列强烈表明它属于腺激肽释放酶家族。人精浆的结构蛋白是精囊分泌的主要蛋白，被前列腺酶快速裂解，这表明这种精囊蛋白可能作为蛋白酶的生理底物。前列腺酶水解含精氨酸和赖氨酸的底物，并且明显偏爱前者。所有测试的合成底物都是该酶的不良底物。合成因子 XIa 底物（焦谷氨酰-脯氨酰-精氨酸-对硝基苯胺）和合成激肽释放酶底物（H-D-脯氨酰-苯丙氨酰-精氨酸-对硝基苯胺）在 23°C 下水解，具有最大比活性。每毫克的 C 值分别为 79 和 34 nmol/min，Km 值分别为 1.0 和 0.45 mM。纤溶酶、胰凝乳蛋白酶和弹性蛋白酶的合成底物要么根本不被酶水解，要么仅水解得很慢。
A 33-kD glycoprotein, known as the "prostate-specific antigen," was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XIa substrate (pyroglutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23.degree. C of 79 and 34 nmol/min per mg and Km values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.