Binding affinity of N-glycans for aromatic amino acid residues: implications for novel interactions between N-glycans and proteins.
This study advances direct evidence of the binding affinity of N-glycans for aromatic amino acid residues. The intrinsic fluorescence intensities of bovine pancreatic RNase A, bovine alpha-lactalbumin, and aromatic amino acids were markedly depressed in solutions (1 mM or so) of free N-glycans of both the high-mannose and complex types. In addition, free N-glycans inhibited the chemical modifications of the solvent-exposed tyrosine and tryptophan residues of these proteins, confirming the affinity of N-glycans for aromatic amino acid residues. The results are discussed in connection with the roles of N-glycans in novel interactions between N-glycans and proteins.
Yamaguchi
H
H
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University, Sakai, Osaka, 599-8531, Japan. simplife@biochem.osakafu-u.ac.jp
Nishiyama
T
T
Uchida
M
M
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001216:Asparagine / Q000737:chemistry / Q000378:metabolism; D001667:Binding, Competitive; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D007768:Lactalbumin / Q000737:chemistry; D010649:Phenylalanine / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013395:Sucrose / Q000378:metabolism; D014364:Tryptophan / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D000596:Amino Acids; D011134:Polysaccharides; D014443:Tyrosine; D010649:Phenylalanine; D013395:Sucrose; D001216:Asparagine; D014364:Tryptophan; D007768:Lactalbumin; D012259:Ribonuclease, Pancreatic