Oxidative refolding of bovine pancreatic RNases A and B promoted by Asn-glycans

Journal of Biochemistry
I NishimuraH Yamaguchi

Abstract

It was previously revealed [Yamaguchi, H. and Uchida, M. (1996) J. Biochem. 120, 474-477] that both intra- and extramolecular high-mannose type Asn-glycans promote the renaturation of reductively denatured bovine pancreatic RNases A and B under oxidation conditions. To characterize the conformational changes of the polypeptides during the renaturation promoted by the intramolecular Asn-glycans, RNase B was compared with its nonglycosylated form, RNase A, as to the features of the regeneration from their reductively denatured species under Cu2+-catalyzed oxidation conditions. The refolding intermediates of RNase B, as compared with those of RNase A, seemed to contain much less impaired disulfide linkages. In agreement with this finding, the proper refolding of RNase B was much faster than that of RNase A, as revealed by the intrinsic fluorescence and 1-anilino-8-naphthalenesulfonate binding of the refolding intermediates. Such a promoting effect was also observed for extramolecular Asn-glycans of the complex as well as of the high-mannose type. In contrast, common mono-, oligo-, and polysaccharides, but not yeast mannan, exhibited much lower stimulatory effects on the oxidative refolding of RNase A.

Citations

Aug 14, 1999·European Journal of Biochemistry·Y KimuraA Sturm
Jan 14, 2011·Bioscience, Biotechnology, and Biochemistry·Mariko KimuraYoshinobu Kimura
Nov 26, 2015·Glycobiology·Himadri Biswas, Rajagopal Chattopadhyaya
Sep 19, 2006·Biophysical Journal·Sharmistha Sinha, Avadhesha Surolia
Feb 14, 2006·Trends in Biochemical Sciences·Nivedita MitraAvadhesha Surolia
Oct 28, 2004·The Journal of Biological Chemistry·Guangtao LiWilliam J Lennarz
Apr 25, 2012·Journal of the American Chemical Society·Christopher R EllisWilliam G Noid

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