从马血白细胞中分离出一种类弹性蛋白酶的蛋白酶及其性质
Isolation and properties of an elastase-like proteinase from horse blood leucocytes.
作者信息
Potempa J
出版信息
Folia Histochem Cytochem (Krakow). 1982;20(1-2):41-52.
The rapid, two steps method of purification of an elastase-like proteinase from cytoplasmic granules of horse leucocytes is described. This enzyme called the proteinase 1 is released easily from isolated granules in the low ionic strength solutions in opposite to the other two molecular forms of which one differs slightly in isoelectric point from the other. The enzyme is a typical neutral proteinase of a broad substrate specificity and wide pH optimum. In a physiological conditions the enzyme is built of two polypeptide chains of molecular weight about 30000 and 20000, respectively.
本文描述了从马白细胞胞质颗粒中快速两步纯化类弹性蛋白酶蛋白酶的方法。这种被称为蛋白酶1的酶在低离子强度溶液中很容易从分离的颗粒中释放出来，这与其他两种分子形式相反，其中一种在等电点上与另一种略有不同。该酶是一种典型的中性蛋白酶，具有广泛的底物特异性和较宽的最适pH值。在生理条件下，该酶由两条分别约为30000和20000分子量的多肽链组成。
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