Ross G T, Marsh J M, Roback D W
J Rheumatol. 1981 Sep-Oct;8(5):710-5.
Extracts containing uridine diphosphate (UDP) glucose dehydrogenase (EC 1.1.1.22) activity were prepared from rheumatoid and from normal human synovial cell lines using previously standardized techniques. Although no significant differences in the enzyme from the 2 sources were detected with respect to activity, substrate affinities, or responses to temperature and pH, these determinations have demonstrated that the enzyme is very sensitive to alterations in these parameters. The ultimate activity of the enzyme in vivo will be dependent upon the extent of the increased temperature, acidity, and altered glucose metabolism in the rheumatoid joint.
使用先前标准化的技术，从类风湿性和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。尽管在活性、底物亲和力或对温度和pH的反应方面未检测到这两种来源的酶有显著差异，但这些测定表明该酶对这些参数的变化非常敏感。该酶在体内的最终活性将取决于类风湿性关节中温度升高、酸度增加和葡萄糖代谢改变的程度。
