Purification and characterization of cytochrome C from camel muscle.
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.
Gorban
A M
AM
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
Izzeldin
O M
OM
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
D003574:Cytochrome c Group