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The cell‐surface iodinatable proteins of Trypanosoma cruzi have been analyzed by two‐dimensional polyacrylamide gel electrophoresis under equilibrium conditions. Antigenic polypeptides were characterized after immunoprecipitation and glycoproteins were identified by means of lectin‐affinity chromatography.

Two glycoproteins, with affinity for concanavalin A, were found to be common to both infective (trypomastigote) and non‐infective (epimastigote) forms: protein 2 (90kDa, pI5.5–6.5) and protein 2 (80kDa, pI5.3‐6.3).

In epimastigotes a specific concanavalin‐A‐binding surface glycoprotein (70kDa, pI5.5) was identified. Trypomastigote forms, on the other hand, presented several specific iodinatable surface components: glycoproteins 3 (85kDa, pI5.5), 4 (85kDa, pI5.0), 6(100kDa, pI6.5), 7 (12kDa, pI6.3), 8 (68kDa, pI6.7) and several minor high‐molecular‐mass acid proteins, all containing glucose and/or …