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猪胰蛋白酶经胃蛋白酶有限度地水解后的活性产物可以用大豆胰蛋白酶抑制剂STI-Sepharose亲和层析方法分离出三种形式的活性分子:K~(**) ,λ~(**)和μ~(**)胰蛋白酶。三者的分子量与母体酶分子β-胰蛋白酶的分子量相同。它们与特异性底物反应时,三者的活性各异。N末端基测定,表明三者N末端氨基酸的不均一性。结果说明,猪胰蛋白酶经胃蛋白酶水解后在一至两个肽键处发生断裂,由于分子内二硫键的连接,并未导致胰蛋白酶肽链的脱落。
The active product of porcine trypsin with limited hydrolysis by pepsin can be isolated by STI-Sepharose affinity chromatography using soybean trypsin inhibitor: K ~ **, λ ~ ** ) And μ ~ (**) trypsin. The three molecular weight and the parent enzyme molecular β-trypsin molecular weight the same. When they react with a specific substrate, the activities of the three are different. N-terminal group determination, indicating the three N-terminal amino acid heterogeneity. The results showed that porcine trypsin by pepsin hydrolysis at one or two peptide bonds at the fracture, due to the intramolecular disulfide bond, did not lead to the loss of the tryptic peptide chain.