人滑液中β-葡萄糖醛酸酶活性的特性
Properties of beta-glucuronidase activity in human synovial fluid.
作者信息
Moro L, de Bernard B, Gonano F
出版信息
Clin Chim Acta. 1975 Dec 15;65(3):371-7. doi: 10.1016/0009-8981(75)90263-6.
The purpose of the present study was to evaluate the properties of beta-glucuronidase (EC 3.2.1.31) in human synovial fluid. It was shown to have a pH requirement of 5.0 and a KM value of about 8.0 - 10(-3) M using phenolphthalein beta-glucuronide as the substrate. At low substrate concentration an endogenous inhibitor is demonstrable. The inhibition is of the competitive type and is removed by proteolytic digestion of synovial fluid, whereas hyaluronidase digestion and addition either of Triton X-100 or of various salts to the assay mixture, are ineffective. The possibility that the inhibitor is a protein from serum is discussed.
本研究的目的是评估人滑液中β-葡萄糖醛酸酶（EC 3.2.1.31）的特性。以酚酞β-葡萄糖醛酸苷为底物时，该酶的最适pH为5.0，KM值约为8.0×10⁻³M。在低底物浓度下，可证明存在一种内源性抑制剂。这种抑制作用属于竞争性类型，通过对滑液进行蛋白水解消化可消除，而透明质酸酶消化以及向测定混合物中添加Triton X-100或各种盐均无效。文中讨论了该抑制剂可能是血清来源蛋白质的可能性。
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