A chaperone-like function of intramolecular high-mannose chains in the oxidative refolding of bovine pancreatic RNase B.
This paper describes a chaperone-like function of the intramolecular N-glycans of bovine pancreatic RNase B. We studied air-oxidative regeneration from reductively denatured species of RNase B and its nonglycosylated form, RNase A. RNase B was reactivated much faster than RNase A, while RNase A was liable to aggregate during the regeneration. An Asn-linked oligosaccharide, Man5GlcNA2Asn, which corresponds to the most predominant sugar chain (ca. 60%) of RNase B, enhanced the reactivation of the denatured RNases A and B. The stimulatory effect of this Asn-oligosaccharide revealed that the N-glycans of RNase B facilitate the transformation of bulky intermediates into folded, compact species.
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University.
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Yamaguchi
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Uchida
D000818:Animals; D002240:Carbohydrate Sequence; D002417:Cattle; D018833:Chaperonins; D007700:Kinetics; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry*; D010084:Oxidation-Reduction; D010179:Pancreas / Q000201:enzymology*; D011134:Polysaccharides; D011489:Protein Denaturation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012260:Ribonucleases / Q000737:chemistry*
D009844:Oligosaccharides; D011134:Polysaccharides; D012260:Ribonucleases; C029600:ribonuclease B; D012259:Ribonuclease, Pancreatic; D018833:Chaperonins