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  • Title: Solubilization and partial purification of two forms of cytochrome P-450 from trout liver microsomes.
    Author: Arinç E, Adali O.
    Journal: Comp Biochem Physiol B; 1983; 76(3):653-62. PubMed ID: 6641180.
    Abstract:
    Liver microsomal cytochrome P-450 content, NADPH-cytochrome c reductase, aniline 4-hydroxylase and ethylmorphine N-demethylase activities of rainbow trout, Salmo gairdneri, were found to be 0.16 (n = 10) nmol P-450/mg protein, 38 (n = 5) units/mg protein, 0.04 (n = 4) nmol p-aminophenol/min/mg protein and 0.174 (n = 3) nmol formaldehyde/min/mg protein, respectively. Trout liver cytochrome P-450 was solubilized by treatment of microsomes with sodium cholate. Chromatography on DEAE-cellulose column yielded two distinct cytochrome P-450 fractions from solubilized microsomes. Cytochrome P-450-I was eluted with Emulgen 913-containing buffer. Application of 0.08 M KCl in Emulgen 913-containing buffer to the DEAE-cellulose column eluted cytochrome P-450-II fraction. Cytochrome P-450-I was further purified on hydroxylapatite column. CO-difference spectrum of dithionite-reduced cytochrome P-450-I gave a peak at 449 nm while the similar spectrum of cytochrome P-450-II showed a maximum absorbance at 451 nm. Monomer molecular weights of cytochrome P-450-I and cytochrome P-450-II were determined by sodium dodecyl sulfate gel electrophoresis and found to be 56,000 and 48,500, respectively.
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