Purification and characterization of the corticosteroid 11 beta-dehydrogenase component of the rat liver 11 beta-hydroxysteroid dehydrogenase complex.
作者： VIJAYA LAKSHMI , CARL MONDER
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摘要: We have proposed that 11 beta-hydroxysteroid dehydrogenase is composed of structurally independent units with beta-dehydrogenase and 11-reductase activities. now report the purification rat liver to apparent homogeneity. Starting microsomes, 800-fold was achieved agarose-NADP affinity chromatography. No accompanied purification. Homogeneity determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis amino acid end-group analysis immunoprecipitation. The terminal methionine. Monomer mol wt 34,000. enzyme found be a glycoprotein. A sequence 40 identified from end. amino-terminal region highly nonpolar. Unlike unpurified microsomal beta-dehydrogenase, which showed curvilinear Eadie plots, homogeneous gave rectilinear plots. Michaelis constants were 1.83 +/- 0.06 microM for corticosterone 17.3 2.24 cortisol. First order rate 10 times greater than cortisol, maximum velocities similar.
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