Matta M S, Henderson P A, Drew H D, Wilbraham A C, Benitez J G, Mudd J M, North D K
J Biol Chem. 1977 Dec 10;252(23):8423-7.
A search for the source of the residual esterase activity of crude lima bean protease inhibitor-binding anhydrochymotrypsin preparations was undertaken. The preparations were found to contain about 40% of protein that possesses 1% (kc/Km) to 12% (kc) of the esterase activity of alpha-chymotrypsin. The active protein was isolated by affinity chromatography on soybean trypsin inhibitor-Sepharose. It appears to be an anhydroenzyme or a mixture of a limited number of anhydroenzymes in which a serine other than the catalytically essential serine-195 of the native enzyme has been converted to dehydroalanine.
对粗制利马豆蛋白酶抑制剂结合脱水胰凝乳蛋白酶制剂中残留酯酶活性的来源进行了探寻。发现这些制剂含有约40%的蛋白质，其具有α-胰凝乳蛋白酶酯酶活性的1%（kc/Km）至12%（kc）。活性蛋白通过在大豆胰蛋白酶抑制剂-琼脂糖上进行亲和层析分离得到。它似乎是一种脱水酶或有限数量脱水酶的混合物，其中天然酶催化必需的丝氨酸-195以外的丝氨酸已转化为脱氢丙氨酸。
