Mosolov V V, Fedurkina N V, Valueva T A
Biokhimiia. 1977 Jul;42(7):1201-11.
Two isoinhibitors (II and III-B) have been isolated from kidney bean (Phaseolus vulgaris L.) in a highly purified state. Both were active against trypsin and chymotrypsin to the same extent. Their amino acid composition is characterized by a high content of half-cystine, aspartic acid (or asparagine) and serine, by the absence of valine, methionine and tryptophan. Glycine and serine were N-terminal in II and III-B respectively. Both isoinhibitors have C-terminal leucine.
已从菜豆（Phaseolus vulgaris L.）中以高纯度状态分离出两种异抑制剂（II和III - B）。两者对胰蛋白酶和糜蛋白酶的活性程度相同。它们的氨基酸组成特点是半胱氨酸、天冬氨酸（或天冬酰胺）和丝氨酸含量高，不含缬氨酸、蛋氨酸和色氨酸。甘氨酸和丝氨酸分别是II和III - B的N末端。两种异抑制剂的C末端均为亮氨酸。
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