AbstractUsing neoglycoproteins, lectine that reconize different sugars, including N‐acetylglucosamine residues, were previously detected in animal cell nuclei. We report herein the isolation of two N‐acetylglucosamine‐binding protein from HL60 cell nuclei:(i) a 22 kDa polypeptide (CBP22) with an isoelectric point of 4.5 was isolated for the first time and (ii) a 70 kDa polypeptide point of 7.8. This latter protein corresponds to the glucose‐binding protein (CBP70) previously isolated, based on the following similsrties:(i) they have the same molecular mass, (ii)they have the same isoelectric point, (iii)they are recognized by antibodies raised against CBP70, and (iv) both are lectins from the C group of Drickamer's classsification. CBP70 appeared to recognized glucose and n‐acetylglucosamine; howeve, its affinity for N‐acetylglucosamine was found to be twice that for glucose. The presence in the nucleus of two nuclear N‐acetylglucosamine‐binding protein and their potential ligands, such as O‐N‐acetylglucosamine glycoproteins, strongly argues for possible intranuclear glycoprotein‐lectine interactions.