Purification and properties of cytochrome c555 from Leishmania donovani.
A hemoprotein present in minute quantities in Leishmania donovani promastigotes was isolated, purified and spectrally characterized as cytochrome c555. Physicochemical characterization revealed electrophoretic mobility of 1.6 X 10(-5) cm2 V-1 s-1, an isoelectric point (pI) of 9.9, a relative molecular weight (Mr) of 11.9 kDa and half-wave potential (Ep) of -1.058 V. Values obtained were compared with those of horse heart cytochrome c subjected to the same analyses. Heme c555 was also prepared and spectrally characterized. The results indicated that leishmanial cytochrome c555 is similar but not identical to its crithidial counterpart.
D000818:Animals; D003574:Cytochrome c Group / Q000032:analysis / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006418:Heme / Q000031:analogs & derivatives / Q000032:analysis; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007893:Leishmania donovani / Q000032:analysis*; D008970:Molecular Weight; D013053:Spectrophotometry
D003574:Cytochrome c Group; C031690:heme C; D006418:Heme; C018887:cytochrome c-555