title: Purification and characterization of cytochrome C from camel muscle.
abstract: Cytochrome C was purified from camel skeletal muscles using ammonium sulphate fractionation and gel filtration on Sephadex G25 and Sephecryl S200 columns. The preparations were pure by SDS-PAGE criteria, with molecular weight of 12,300 Dalton. The electrophoretic mobility of camel cytochrome C was the same as that of the horse heart. The spectral characteristics of the isolated cytochrome C were also investigated.
authors.affiliation: Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
authors.forename: A M
authors.initials: AM
authors.lastname: Gorban
authors.forename: O M
authors.initials: OM
authors.lastname: Izzeldin
mesh_terms: D000818:Animals; D002162:Camelus / Q000378:metabolism*; D002850:Chromatography, Gel; D003574:Cytochrome c Group / Q000737:chemistry* / Q000302:isolation & purification*; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D009132:Muscles / Q000378:metabolism*; D013053:Spectrophotometry
chemical_list: D003574:Cytochrome c Group