[詹氏放线菌118来源的胰蛋白酶胞外蛋白抑制剂的稳定性和特异性]

[Stability and specificity of extracellular protein inhibitor for trypsin from Actinomyces janthinus 118].

作者信息

Andreeva N A, Chermenskiĭ D N

出版信息

Biokhimiia. 1979 May;44(5):838-43.

Abstract

Some properties of protein inhibitor for trypsin (TI) from Act. janthinus 118 were studied. It was shown that TI has an antitrypsin activity within a wide pH range with a maximum at about 9,5. At 4 degrees and 20 degrees C TI is stable for 24 hours within the pH range of 6,0--11,0. At 100 degrees C TI is more stable in the slightly acid region of pH than at neutral or alkaline conditions. Trypsin and chymotrypsin inactivate the inhibitor for 8 hours. TI inhibits trypsin, fibrinolysin, subtilisin, pronase and terrilytin, but have no effect on chymotrypsin, thrombin, papain and pepsin. The dissociation constants for the trypsin-inhibitor complex were found to be 1,7.10-8 M, 4,1.10-9 M and 2,4.10-10 M, with casein, p-nitroanilide benzoylarginine and tosylarginine methyl ester used as substrates, respectively. The corresponding dissociation rate constants for the subtilisin-inhibitor complex were equal to 1.10-9 M and 4.10-10 M with casein and carbobenzoxy-L-alanyl-L-alanyl-L-leucin p-nitroanilide used as substrates, respectively.

摘要

对来自Act. janthinus 118的胰蛋白酶蛋白抑制剂（TI）的一些特性进行了研究。结果表明，TI在较宽的pH范围内具有抗胰蛋白酶活性，在pH约为9.5时活性最高。在4℃和20℃下，TI在pH 6.0 - 11.0范围内24小时保持稳定。在100℃时，TI在pH略酸性区域比在中性或碱性条件下更稳定。胰蛋白酶和糜蛋白酶可使该抑制剂失活8小时。TI抑制胰蛋白酶、纤维蛋白溶酶、枯草杆菌蛋白酶、链霉蛋白酶和土曲霉蛋白酶，但对糜蛋白酶、凝血酶、木瓜蛋白酶和胃蛋白酶无作用。以酪蛋白、对硝基苯胺苯甲酰精氨酸和甲苯磺酰精氨酸甲酯分别作为底物时，胰蛋白酶 - 抑制剂复合物的解离常数分别为1.7×10⁻⁸M、4.1×10⁻⁹M和2.4×10⁻¹⁰M。以酪蛋白和苄氧羰基 - L - 丙氨酰 - L - 丙氨酰 - L - 亮氨酰对硝基苯胺分别作为底物时，枯草杆菌蛋白酶 - 抑制剂复合物的相应解离速率常数分别为1×10⁻⁹M和4×10⁻¹⁰M。