Characterization of a protein fraction containing cytochromes b and c1 from mitochondria of Leishmania tarentolae.
A soluble red band fraction was obtained from Leishmania tarentolae cells by sucrose gradient sedimentation of a Triton X-100 lysate. Spectral analysis indicated that cytochrome b was present in the red band: the reduced minus oxidized difference spectra revealed absorption maxima at 562,527, and 431 nm at room temperature and 562, 530, and 422 nm at 77K. In addition, a 28-kDa protein was identified in this fraction which retained heme-associated peroxidase activity even after denaturation on SDS-polyacrylamide gels. The amino acid composition of this protein showed a strong similarity to cytochrome c1 of both bovine and yeast.
Shaw
J M
JM
Department of Biology, University of California, Los Angeles.
Simpson
L
L
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002499:Centrifugation, Density Gradient; D003573:Cytochrome b Group / Q000032:analysis*; D003574:Cytochrome c Group / Q000031:analogs & derivatives*; D003575:Cytochromes c1 / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D007891:Leishmania / Q000032:analysis* / Q000648:ultrastructure; D008928:Mitochondria / Q000032:analysis*; D013057:Spectrum Analysis
D000596:Amino Acids; D003573:Cytochrome b Group; D003574:Cytochrome c Group; D003575:Cytochromes c1