作者: J. de VELLIS , J.F. McGINNIS , G.A.M. BREEN , P. LEVEILLE , K. BENNETT
DOI: 10.1016/B978-0-12-250450-1.50027-2
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摘要: The data presented clearly demonstrate that the induction of glycerol phosphate dehydrogenase (GPDH) by cortisol in C6 cells is due to an increased rate synthesis without alteration degradation enzyme, thus resulting a greater number molecules. Similarly, we have shown immunotitration, Ouchterlony double diffusion, gel permeation chromatography, pH optimun, heat lability and polyacrylamide electrophoresis GPDH brains normal (induced) hypophysectomized (uninduced) rats identical. Thus vivo as cell culture, hormonal regulation activity brought about change molecules, not their catalytic efficiency. Similar questions now arise mRNA for GPDH, i.e., influence hydrocortisone on its efficiency translation. Since brain identical enzyme present muscle liver, mechanism specificity intrinsic property tissue rather than related itself such coding different structural genes.