URIDINE-DIPHOSPHATE GLUCOSE-DEHYDROGENASE IN NORMAL HUMAN SYNOVIAL-CELLS IN CULTURE

  • 1 January 1979
    • journal article
    • research article
    • Vol. 6  (5) , 489-496
Abstract
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 .times. 10-3. IU/mg protein. The Km UDP-glucose was estimated as 3.90 .+-. 1.56 .times. 10-5 M and the Km NAD+ was estimated as 1.72 .+-. 0.60 .times. 10-4 M. Maximum catalytic activity occurred in a temperature range of 55.degree. C-68.degree. 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.