Solubilization and partial purification of cytochrome P-450s from trout liver microsomes.

Date

1982

Author

Adalı, Orhan

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https://hdl.handle.net/11511/5433

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Graduate School of Natural and Applied Sciences, Thesis

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SOLUBILIZATION AND PARTIAL-PURIFICATION OF 2 FORMS OF CYTOCHROME-P-450 FROM TROUT LIVER-MICROSOMES ARINC, E; Adalı, Orhan (Elsevier BV, 1983-01-01) 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 f...
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Citation Formats

O. Adalı, “Solubilization and partial purification of cytochrome P-450s from trout liver microsomes.,” Middle East Technical University, 1982.