Pham T C, Leluk J, Wilusz T, Polanowski A
Acta Biochim Pol. 1985;32(4):319-28.
Two trypsin inhibitors, CPPTI-I and CPPTI-II of Mr 3 250 and 7 850, respectively, were isolated from resting white bush seeds. Both inhibitors are cysteine-rich proteins. In addition to trypsin, they inhibit a trypsin-like enzyme isolated from Streptomyces griseus proteinase but they do not act on chymotrypsin, kallikrein or subtilopeptidase A. The isolated inhibitors contain a lysine residue in position P1 of the reactive site.
从休眠的白布什种子中分离出两种胰蛋白酶抑制剂,分别是分子量为3250的CPPTI-I和分子量为7850的CPPTI-II。这两种抑制剂都是富含半胱氨酸的蛋白质。除了胰蛋白酶外,它们还抑制从灰色链霉菌蛋白酶中分离出的一种类胰蛋白酶,但对胰凝乳蛋白酶、激肽释放酶或枯草杆菌肽酶A没有作用。分离出的抑制剂在活性位点的P1位置含有一个赖氨酸残基。