Oliva M L, Sampaio M U, Sampaio C A
Departamento de Bioquímica, Escola Paulista de Medicine, São Paulo, Brasil.
Braz J Med Biol Res. 1987;20(6):767-70.
Two types of proteinase inhibitors were purified from Enterolobium contortisiliquum beans. The inhibitor of serine-proteinases inhibited trypsin (Ki = 5 nM), chymotrypsin (Ki = 10 nM) and plasma kallikrein, but not tissue kallikreins. The molecular weight is approximately 23 kDal and two polypeptide chains are detected after reduction. The second inhibitor with activity directed against SH-proteinases was isolated by CM-papain-Sepharose. The molecular weight is approximately 60 kDal and only one polypeptide chain was detected after reduction. Papain (Ki = 0.6 nM) and bromelain are inhibited.
从扭荚苏木豆中纯化出了两种蛋白酶抑制剂。丝氨酸蛋白酶抑制剂可抑制胰蛋白酶(Ki = 5 nM)、胰凝乳蛋白酶(Ki = 10 nM)和血浆激肽释放酶,但不抑制组织激肽释放酶。其分子量约为23 kDal,还原后可检测到两条多肽链。通过CM-木瓜蛋白酶-琼脂糖分离出了第二种针对巯基蛋白酶具有活性的抑制剂。其分子量约为60 kDal,还原后仅检测到一条多肽链。木瓜蛋白酶(Ki = 0.6 nM)和菠萝蛋白酶受到抑制。