The identification of glycoproteins in complex mixtures derived from human blood is important to indicate pathological state. Schistomiasis is a serious public health problem in several regions around the world as South America including Brazil (mainly in the Northeast) and Africa. This disease is characterized by serious hepatic lesions. The study of abnormal plasma proteins produced by the liver associated with this patological condition seems to be valuable in diagnosis. Our work intends to identify plasma glycoproteins using the comercial  lectin Concanavalin A (Con-A) and Cramoll lectin, isolated from Cratylia mollis seeds, a tipical leguminous from the Northeast, in order to compare plasma proteins from controls and schistossomiasis patients. After the affinity chromatography fractions eluted from Con A and Cramoll columns were subjected to bidimensional electrophoresis. Then, all resolved protein spots were first excised, trypsin digested, analized by mass spectrometry MALDI-TOF and finally the spectrum of peptides was performed by MASCOT program databases. Comparative analyses between controls using Con A and Cramoll lectin demonstrated that even with the same carbohydrate specificity they adsorbed different plasma glycoproteins. Using fraction eluted map as standard, the spot pattern in three maps from controls using Con A lectin showed hemopexin, haptoglobin, haptoglobin alpha-2, fibrinogen beta chain, beta-2-glycoprotein, alpha 1-beta-glycoprotein, alpha 1–antitripsyn, antithrombin, erythropoietin, albumin, transferrin, immunoglobulin alpha-2 heavy chain, immunoglobulin alpha-1 heavy chain, immunoglobulin alpha-1 chain C region, crystal structure of Fab fragment from human monoclonal Igm cold agglutinin, crystal structure of  the IgA  module complexed with human serum chain A, immunoglobulin kappa chain constant region and immunoglobulin kappa light chain. Using the same parameters plasma of schistossomiasis patients showed similar results except for the absence of erythropoietin and presence of other proteins and fractions including complement component 3, immunoglobulin G Kappa chain,  immunoglobulin kappa light chain VLJ, histidine-rich glycoprotein, immunoglobulin Aalpha1, immunoglobulin kappa-chain VK-1, immunoglobulin G kappa and Immunoglobulin Gamma-1 chain C.   Suported by CnPq, FACEPE and PADCT.