SOLUBILIZATION AND PARTIAL-PURIFICATION OF 2 FORMS OF CYTOCHROME-P-450 FROM TROUT LIVER-MICROSOMES

Date

1983-01-01

Author

ARINC, E
Adalı, Orhan

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1. 1. Liver microsomal cytochrome P-450 content, NADPH-cytochrome reductase, aniline 4-hydroxylase and ethylmorphine activities of rainbow trout, Salmo gairdneri, were found to be 0.16 () nmol P-450/mg protein, 38 () units/mg protein, 0.04 () nmol protein and 0.174 ( ) nmol formaldehyde/min/mg protein, respectively. 2. 2. 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. 3. 3. 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.

Subject Keywords

Biochemistry, Physiology, Molecular Biology, General Medicine

URI

https://hdl.handle.net/11511/43072

Collections

Department of Biology, Article