Hepatic microsomal NADPH-cytochrome P-450 reductase from little skate, Raja erinacea. Comparison of thermolability and other molecular properties with a mammalian enzyme

Chemico-biological Interactions
R J PohlR M Philpot

Abstract

Components of little skate (an elasmobranch) and rabbit hepatic microsomal cytochrome P-450 dependent monooxygenase systems were examined for differences which might explain the decreasing xenobiotic-metabolizing activity of little skate microsomes assayed at temperatures above 30 degrees C. The proportion of saturated fatty acids in microsomal lipids and the habitat temperature are both lower in skate as compared to rabbit, which is consistent with the known adaptive pattern. The more thermolabile enzyme of the skate system in microsomal preparations is NADPH-cytochrome P-450 reductase. The optimal assay temperature for purified skate reductase (30 degrees C) is 10 degrees C lower than that for the purified rabbit reductase. The purified skate reductase differs from rabbit reductase in monomeric molecular weight, in peptides produced by partial proteolysis, in immunochemical properties, but not in flavin content.

References

Dec 11, 1979·Biochemistry·P ArgosJ D Tratschin
Dec 1, 1978·Chemico-biological Interactions·P W AlbroL D Lawson
Mar 19, 1976·Biochimica Et Biophysica Acta·W Duppel, V Ullrich
May 1, 1973·Analytical Biochemistry·E J Faeder, L M Siegel
Jul 1, 1974·Physiological Reviews·J R Hazel, C L Prosser
Aug 21, 1980·Biochimica Et Biophysica Acta·C R WolfR M Philpot
Jan 1, 1949·Acta Pathologica Et Microbiologica Scandinavica·O OUCHTERLONY

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