Slaughter D, Schoeffel S, Triplett E
Cell Differ. 1977 Dec;6(5-6):273-84. doi: 10.1016/0045-6039(77)90002-1.
Amphibian embryo chymotrypsin and papain inhibitor (ACPI) purified by the procedure described in this paper produces a single band on sodium dodecyl sulfate (SDS) gel electrophoresis and a single peak on Sephadex G-75 chromatography. Except for its enzyme specificity, ACPI is very similar to amphibian embryo trypsin inhibitor (ATI). Its molecular weight is about 10,500 and its amino acid composition is typical of many naturally occurring protease inhibitors. Inhibition develops slowly, is retarded by the presence of substrate and is temporary. ACPI is localized in the yolk platelets and its disappearance both from whole embryos and from select tissue types corresponds closely with that of ATI. Possible roles for amphibian embryo proteases and protease inhibitors in development are discussed.
通过本文所述方法纯化的两栖类胚胎糜蛋白酶和木瓜蛋白酶抑制剂（ACPI）在十二烷基硫酸钠（SDS）凝胶电泳上产生一条带，在葡聚糖凝胶G - 75层析上出现一个峰。除了酶特异性外，ACPI与两栖类胚胎胰蛋白酶抑制剂（ATI）非常相似。其分子量约为10500，氨基酸组成是许多天然存在的蛋白酶抑制剂的典型组成。抑制作用发展缓慢，受底物存在的阻碍且是暂时的。ACPI定位于卵黄小板中，其从整个胚胎和特定组织类型中的消失与ATI的消失密切对应。文中讨论了两栖类胚胎蛋白酶和蛋白酶抑制剂在发育中的可能作用。
