培养的正常人滑膜细胞中的尿苷二磷酸葡萄糖脱氢酶
Uridine diphosphate glucose dehydrogenase in normal human synovial cells in culture.
作者信息
Ross G T, Marsh J M, Roback D W
出版信息
J Rheumatol. 1979 Sep-Oct;6(5):489-96.
Extracts containing uridine diphosphate (UDP) glucose dehydrogenase (EC 1.1.1.22) activity were prepared from 5 normal human synovial cell lines and sources of variation in the method determined. The mean catalytic activity of UDP-glucose dehydrogenase from the 5 extracts was 12.0 +/- 2.4 x 10(-3) International Units/mg protein. The KmUDP-glucose was estimated as 3.90 +/- 1.56 x 10(-5) M and the KmNAD+ was estimated as 1.72 +/- 0.60 x 10(-4) M. Maximum catalytic activity occurred in a temperature range of 55 degrees C-68 degrees C and in a pH range of 8.1-8.4. The mechanistic implications of these data in the normal human diarthrodial joint are discussed.
从5种正常人滑膜细胞系中制备了含有尿苷二磷酸（UDP）葡萄糖脱氢酶（EC 1.1.1.22）活性的提取物，并确定了该方法中的变异来源。5种提取物中UDP-葡萄糖脱氢酶的平均催化活性为12.0±2.4×10⁻³国际单位/毫克蛋白质。UDP-葡萄糖的Km值估计为3.90±1.56×10⁻⁵M，NAD⁺的Km值估计为1.72±0.60×10⁻⁴M。最大催化活性出现在55℃-68℃的温度范围内和8.1-8.4的pH范围内。讨论了这些数据在正常人滑膜关节中的机制意义。
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