Polanowski A, Wilusz T, Nienartowicz B, Cieślar E, Słomińska A, Nowak K
Acta Biochim Pol. 1980;27(3-4):371-82.
Trypsin inhibitor from squash (Cucurbita maxima) seed was extracted with 0.1 M-acetate buffer, pH 4.5, purified on immobilized trypsin, and separated by SE-Sephadex C-50 chromatography into three active fractions. All of them inhibited trypsin to the same extent, showed no antichymotrypsin or antikallikrein activity, had a similar molecular weight (about 3300), and contained no tryptophan, phenylalanine or threonine. The partial amino acid sequence of tryptic and peptic peptides of fraction III was determined by Edman degradation procedure.
从南瓜（笋瓜）种子中提取的胰蛋白酶抑制剂，用pH 4.5的0.1M醋酸盐缓冲液提取，在固定化胰蛋白酶上进行纯化，然后通过SE - Sephadex C - 50色谱法分离成三个活性组分。它们对胰蛋白酶的抑制程度相同，不显示抗胰凝乳蛋白酶或抗激肽释放酶活性，分子量相似（约3300），并且不含色氨酸、苯丙氨酸或苏氨酸。通过埃德曼降解法测定了组分III的胰蛋白酶和胃蛋白酶肽段的部分氨基酸序列。
