Purification of intracellular forms of Plasmodium chabaudi and their interactions with the erythrocyte membrane and with serum albumin.

A procedure using bovine serum albumin gradients was developed for the separation of P. chabaudi-infected mouse erythrocytes from uninfected cells. This procedure can be used for the purification of erythrocytes containing different developmental stages of the parasite. The purified parasites were able to synthesize in vitro all the proteins that they are capable of synthesizing in vivo. The intracellular forms of P. chabaudi were found to be associated with erythrocyte membrane components and this associated membrane was shown to lack glycophorin. The free parasites bound albumin from serum; this binding, which showed some specificity with respect to the origin of the albumin, might play a role in the stabilization or protection of the extracellular parasites.