血链球菌IgA蛋白酶的检测及特性
Assay and properties of IgA protease of Streptococcus sanguis.
作者信息
Plaut A G, Gilbert J V, Heller I
出版信息
Adv Exp Med Biol. 1978;107:489-95. doi: 10.1007/978-1-4684-3369-2_55.
An assay procedure for streptococcal IgA protease is described which uses isotopically labelled human serum IgA as substrate. Enzyme activity was monitored by the radioactive counts in the Fab alpha product, which was separated from other components in the digestion mixture by electrophoresis. Cleavage of IgA was linear with respect to time using catalytic amounts of the enzyme. Km was calculated to be 5.5 X 10(-6)M, pH optimum 6.0-7.0 at 37 degrees C, and the enzyme was fully inactivated at low concentrations of the metal chelator ethylenediaminetetraacetic acid.
本文描述了一种链球菌IgA蛋白酶的检测方法，该方法使用同位素标记的人血清IgA作为底物。通过Fabα产物中的放射性计数监测酶活性，该产物通过电泳与消化混合物中的其他成分分离。使用催化量的酶时，IgA的裂解与时间呈线性关系。计算得出Km为5.5×10⁻⁶M，在37℃时最适pH为6.0 - 7.0，并且该酶在低浓度的金属螯合剂乙二胺四乙酸作用下完全失活。
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