HUMAN PROSTATIC GASTRICSINOGEN - THE PRECURSOR OF SEMINAL FLUID ACID PROTEINASE
HUMAN PROSTATIC GASTRICSINOGEN - THE PRECURSOR OF SEMINAL FLUID ACID PROTEINASE
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DOI：
10.1016/0003-9861(81)90158-2
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发表时间：
1981-01-01
影响因子：
3.9
通讯作者：
WARD, PH
中科院分区：
文献类型：
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作者：
CHIANG, L;CONTRERAS, L;WARD, PH
用DEAE-cellulose、DEAE-SephadexA-50、poly-L-lysine-Sepharose 4 B和N-acetyl-L-phenylalanyl-L-tyrosine-Sepharose 4 B亲和层析从人前列腺组织中分离纯化出一种胃腺素原样酸性蛋白酶前体。活性酶在pH 1.0和3.0下水解酸变性Hb，而其它2个活性组分仅显示pH 3.0活性，并且类似于组织蛋白酶D（EC 3.4.23.5）。最适pH值，凝乳活性，对合成底物的特异性，胃酶抑制素的抑制，和MW强烈表明，前列腺衍生的酶是相同的精液和胃液胃泌素。
A gastricsinogen-like acid proteinase precursor was purified by DEAE-cellulose, DEAE-Sephadex A-50, poly-L-lysine-Sepharose 4B and N-acetyl-L-phenylalanyl-L-tyrosine-Sepharose 4B affinity chromatography from human prostates. The active enzyme hydrolyzes acid-denatured Hb at pH 1.0 and 3.0 whereas 2 other active fractions only showed the pH 3.0 activity and resembled cathepsin D (EC 3.4.23.5). The pH optimum, milk-clotting activity, specificity toward synthetic substrates, inhibition by pepstatin, and MW strongly suggest that the prostatic-derived enzyme is identical to seminal fluid and to gastric juice gastricsin.