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Identification of two nuclear N‐acetylglucosamine‐binding proteins
Author(s) -
Felin Murielle,
DoyennetteMoyne MarieAgnès,
Hadjsahraoui Yasmina,
Aubery Michèle,
Hubert Jean,
Sève AnniePierre
Publication year - 1994
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240560413
Subject(s) - n acetylglucosamine , identification (biology) , computational biology , chemistry , biology , biochemistry , ecology , enzyme
Using 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.