Mar 1, 1993

Cytochrome P-450 in liver microsomes of streptozotocin-induced diabetic rats: purification and characterization

Biochimica Et Biophysica Acta
A TodaH Shimeno


Two diabetes-inducible forms of cytochrome P-450, named P-450ST-1 and -ST-2, were purified from the liver microsomes of streptozotocin-diabetic male rats by sodium cholate solubilization, octylamino-Sepharose 4B chromatography and high-performance liquid chromatography with DEAE-5PW and hydroxyapatite columns. The purified P-450 forms gave a single band each on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with an apparent molecular weight of 48,500 for P-450ST-1 or 48,000 for P-450ST-2. The CO-reduced spectral maxima of P-450ST-1 and -ST-2 were at 451 nm. The two cytochromes had the low-spin state of heme in the oxidized form. Both P-450ST-1 and -ST-2 catalyzed the metabolism of aniline, benzphetamine, p-nitroanisole, testosterone and aminopyrine. However, the catalytic activity of P-450ST-2 for these substrates was apparently higher than that of ST-1. Analyses of the NH2-terminal amino-acid sequence and Western immunoblot showed that P-450ST-1 and -ST-2 differed structurally from each other. The catalytic activities, molecular weights, NH2-terminal sequences and/or immunochemical properties of P-450ST-1 and -ST-2 did not agree with those of the other cytochrome P-450 forms purified from diabetic rats previously.

Mentioned in this Paper

Cytochrome P-450 Oxygenase
Microsomes, Liver
Western Blot
Streptozotocin Diabetes
High Pressure Liquid Chromatography Procedure
Enzyme Induction
Ion-Exchange Chromatography Procedure
Rats, Wistar

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