Abramson C, Friedman H
J Bacteriol. 1969 Feb;97(2):715-8. doi: 10.1128/jb.97.2.715-718.1969.
Partially purified staphylococcal hyaluronidase was studied with respect to its electrophoretic properties by the use of starch slurry or semisolid Noble agar as a matrix. The polarity of enzyme activity was found to be cathodal on starch and anodal on agar gel. The electrophoretic migration of the partially purified enzyme on starch, as a function of pH, suggested that the enzyme has an isoelectric point of pH 9.5 to 10.
使用淀粉浆或半固体诺布尔琼脂作为基质,对部分纯化的葡萄球菌透明质酸酶的电泳特性进行了研究。发现酶活性的极性在淀粉上为阴极,在琼脂凝胶上为阳极。部分纯化的酶在淀粉上的电泳迁移作为pH的函数表明,该酶的等电点为pH 9.5至10。