Purification and properties of cytochrome c555 from Leishmania donovani.

Abstract A hemoprotein present in minute quantities in Leishmania donovani promastigotes was isolated, purified and spectrally characterized as cytochrome c 555 . Physicochemical characterization revealed electrophoretic mobility of 1.6 × 10 −5 cm 2 V −1 s −1 , an isoelectric point (p I ) of 9.9, a relative molecular weight ( M r ) of 11.9 kDa and half-wave potential ( E p ) of −1.058 Values obtained were compared with those of horse heart cytochrome c subjected to the same analyses. Heme c 555 was also prepared and spectrally characterized. The results indicated that leishmanial cytochrome c 555 is similar but not identical to its crithidial counterpart.