A method for purifying a glycosylated recombinant protein of interest from a contaminant, comprising: (a) loading onto a Protein A matrix, at about neutral pH, a host cell culture supernatant or filtrate comprising the glycosylated recombinant protein of interest (POI) and a galectin host cell protein (HCP) contaminant, wherein the POI comprises the C H 2 and C H 3 domains of an immunoglobulin Fc domain and one or more terminal beta-galactosyl residues to which the galectin-3 contaminant is reversibly bound; (b) washing the Protein A matrix that has the POI bound to it, with a buffer at about pH 6.0-6.5, comprising 1-3 M calcium chloride; (c) eluting the POI from the Protein A matrix with a buffer comprising citric acid or a citrate salt below about pH 4 into an eluant pool, and: (i) if the eluant pool is more basic than the pH range of pH 3.3-3.7, titrating the eluant pool to pH 3.3-3.7 with citric acid, and (ii) optionally, keeping the eluant pool at pH 3.3-3.7 for a period sufficient for viral inactivation; (d) binding the POI in the eluant pool from (c) to a cation exchange matrix in a low conductivity buffer of about 2-15 mS, at pH 5.0-5.5; (e) eluting the POI from the cation exchange matrix with an electrolyte concentration gradient of increasingly higher conductivity, up to about 40-100 mS, into a CEX eluant pool; and (f) loading the CEX eluant pool onto a hydrophobic interaction chromatography (HIC) matrix in a high conductivity buffer at pH 5.0-6.0 and washing the HIC matrix, whereby the POI is separated from the galectin HCP contaminant. (a) loading onto a Protein A matrix, at about neutral pH, a host cell culture supernatant or filtrate comprising the glycosylated recombinant protein of interest (POI) and a galectin host cell protein (HCP) contaminant, wherein the POI comprises the C H 2 and C H 3 domains of an immunoglobulin Fc domain and one or more terminal beta-galactosyl residues to which the galectin-3 contaminant is reversibly bound; (b) washing the Protein A matrix that has the POI bound to it, with a buffer at about pH 6.0-6.5, comprising 1-3 M calcium chloride; (c) eluting the POI from the Protein A matrix with a buffer comprising citric acid or a citrate salt below about pH 4 into an eluant pool, and: (i) if the eluant pool is more basic than the pH range of pH 3.3-3.7, titrating the eluant pool to pH 3.3-3.7 with citric acid, and (ii) optionally, keeping the eluant pool at pH 3.3-3.7 for a period sufficient for viral inactivation; (i) if the eluant pool is more basic than the pH range of pH 3.3-3.7, titrating the eluant pool to pH 3.3-3.7 with citric acid, and (ii) optionally, keeping the eluant pool at pH 3.3-3.7 for a period sufficient for viral inactivation; (d) binding the POI in the eluant pool from (c) to a cation exchange matrix in a low conductivity buffer of about 2-15 mS, at pH 5.0-5.5; (e) eluting the POI from the cation exchange matrix with an electrolyte concentration gradient of increasingly higher conductivity, up to about 40-100 mS, into a CEX eluant pool; and (f) loading the CEX eluant pool onto a hydrophobic interaction chromatography (HIC) matrix in a high conductivity buffer at pH 5.0-6.0 and washing the HIC matrix, whereby the POI is separated from the galectin HCP contaminant. <EOS>