Entamoeba histolytica HM1:IMSS traphozoites were able to utilize human
hemoglobin but not hemin as a sole iron source to flow in vitro. Prot
eases from crude extracts of E. histolytica degraded human, porcine, a
nd bovine hemoglobins at pH 7.0. These proteolytic activities were fou
nd by electrophoresis in SDS-polyacrylamide gels copolymerized with he
moglobin, with apparent molecular weights of 116, 82, and 21 kDa, the
82-kDa protein being the most active protease against this substrate.
The proteases were classified in the cysteine group since the activiti
es were inhibited by trans-epoxysuccinylleucyiamido(4-guanidino)butane
, p-hydroxymercuribenzoate, iodoacetate, and N-ethylmaleimide and acti
vated with dithiothreitol. Other pathogenic strains of E. histolytica
showed the same pattern of hemoglobinases. These hemoglobin-degrading
proteases could be playing an important role in iron acquisition by E.
histolytica. (C) 1998 Academic Press.