Premium
Purification and characterization of cytochrome C from camel muscle
Author(s) -
Gorban Ali M. S.,
Izzeldin Omar M.
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900202003
Subject(s) - sephadex , cytochrome c , size exclusion chromatography , chemistry , fractionation , cytochrome , chromatography , horse , biochemistry , biology , mitochondrion , enzyme , paleontology
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 12300 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.