This review summarizes the use of biospecific chromatography techniques in the purification of mammalian glycosyltransferases. Ligands that are analogues of donor or acceptor substrates have been linked to cyanogen bromide-activated agarose for use as affinity adsorbents. Immobilized lectins have been employed to recognize the carbohydrate moieties of glycosyltransferase and remove them from complex mixtures. The application of these methods has permitted extensive purification of many membrane-bound glycosyltransferases, some to homogeneity.