Work

Cytochrome P-450cam

Year: 1974

Type: article

Abstract: Crystalline cytochrome P-450cam, the oxygen- and sub- strate-reactive component of a selective methylene 5-exo-hydroxylase, has been prepared from camphor-induced cells of Pseudomonas putida, strain PpG786, by two similar procedures. The first involved autolysis, DEAE-cellulose chromatography, ammonium sulfate fractionation, Sephadex G-75 filtration, calcium phosphate gel chromatography, and crystallization from ammonium sulfate. Procedure II involved Bio-Gel P-150 filtration, DEAE-Sephadex and DEAE-cellulose chromatography, and ammonium sulfate fractionalization. The purified cytochrome P-450cam has a molecular weight in the range of 44,000 to 46,000, depending upon the method of determination. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the protein moiety is composed of a single polypeptide.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)43095-0

Authors: C-A. Yu, I.C. Gunsalus, M. Katagiri, K. Suhara, S. Takemori

Institutions: University of Illinois Urbana-Champaign, University of Illinois System, Kanazawa University

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1595328936

FWCI: 23.21

Cites: 39

Cited by: 163

Related to: 10