Identification of two nuclear N-acetylglucosamine-binding proteins |
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Authors: | Murielle Felin,Marie-Agn s Doyennette-Moyne,Yasmina Hadj-sahraoui,Mich le Aubery,Jean Hubert,Annie-Pierre S ve |
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Affiliation: | Murielle Felin,Marie-Agnès Doyennette-Moyne,Yasmina Hadj-sahraoui,Michèle Aubery,Jean Hubert,Annie-Pierre Sève |
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Abstract: | 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. |
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Keywords: | lectine nucleus HL60 affinity chromatograph glycoprotein |
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