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Volumn 120, Issue 3, 1996, Pages 474-477

A chaperone-like function of intramolecular high-mannose chains in the oxidative refolding of bovine pancreatic RNase B

Author keywords

Asn linked oligosaccharide; Asn linked oligosaccharide function; Glycoprotein; Protein folding; Ribonuclease B

Indexed keywords

CHAPERONE; MANNOSE; PANCREAS ENZYME; RIBONUCLEASE; RIBONUCLEASE A;

EID: 0029783697     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021435     Document Type: Article
Times cited : (32)

References (22)
  • 1
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural aspects
    • Lis, H. and Sharon, N. (1993) Protein glycosylation. Structural aspects. Eur. J. Biochem. 218, 1-27
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 2
    • 0025876740 scopus 로고
    • Protein folding: Local structures, domains, subunits, and assemblies
    • Jaenicke, R. (1991) Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30, 3147-3161
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 3
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T. and Helenius, A. (1992) Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117, 505-513
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 4
    • 0015874675 scopus 로고
    • Conformational studies on a glycosylated bovine pancreatic ribonuclease
    • Puett, D. (1973) Conformational studies on a glycosylated bovine pancreatic ribonuclease. J. Biol. Chem. 248, 3566-3572
    • (1973) J. Biol. Chem. , vol.248 , pp. 3566-3572
    • Puett, D.1
  • 5
    • 0023645327 scopus 로고
    • The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate
    • Graft, R., Lang, K., Vogl, H., and Schmid, F.X. (1987) The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate. J. Biol. Chem. 262, 10624-10629
    • (1987) J. Biol. Chem. , vol.262 , pp. 10624-10629
    • Graft, R.1    Lang, K.2    Vogl, H.3    Schmid, F.X.4
  • 6
    • 0027732562 scopus 로고
    • Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: Studies by the combined use of spectroscopy and gel-filtration size analysis
    • Nagai, K., Shibata, K., and Yamaguchi, H. (1993) Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: Studies by the combined use of spectroscopy and gel-filtration size analysis. J. Biochem. 114, 830-834
    • (1993) J. Biochem. , vol.114 , pp. 830-834
    • Nagai, K.1    Shibata, K.2    Yamaguchi, H.3
  • 7
    • 0023096228 scopus 로고
    • Heterogeneity of bovine corneal proteokeratan sulfate
    • Saitoh, F. and Yamaguchi, H. (1987) Heterogeneity of bovine corneal proteokeratan sulfate. J. Biochem. 101, 453-463
    • (1987) J. Biochem. , vol.101 , pp. 453-463
    • Saitoh, F.1    Yamaguchi, H.2
  • 8
    • 0014959662 scopus 로고
    • A calorimetric study of thermally induced conformational transition of ribonuclease A and certain of its derivatives
    • Tseng, T.Y., Hearn, R.P., Wrathall, O.P., and Sturtevant, J.M. (1970) A calorimetric study of thermally induced conformational transition of ribonuclease A and certain of its derivatives. Biochemistry 9, 2666-2677
    • (1970) Biochemistry , vol.9 , pp. 2666-2677
    • Tseng, T.Y.1    Hearn, R.P.2    Wrathall, O.P.3    Sturtevant, J.M.4
  • 9
    • 0027413488 scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A. 1. Steady state distribution
    • Rothwarf, D.M. and Scheraga, H.A. (1993) Regeneration of bovine pancreatic ribonuclease A. 1. Steady state distribution. Biochemistry 32, 2671-2679
    • (1993) Biochemistry , vol.32 , pp. 2671-2679
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 10
    • 0043140825 scopus 로고
    • The carbohydrate units of ovalbumin: Complete structures of three glycopeptides
    • Conchie, J. and Strachan, I. (1978) The carbohydrate units of ovalbumin: Complete structures of three glycopeptides. Carbohydr. Res. 63, 193-213
    • (1978) Carbohydr. Res. , vol.63 , pp. 193-213
    • Conchie, J.1    Strachan, I.2
  • 11
  • 12
    • 0001041039 scopus 로고
    • Spectro-photometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate
    • Crook, E.M., Mathias, A.P., and Rabin, B.R. (1960) Spectro-photometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate. Biochem. J. 74, 234-238
    • (1960) Biochem. J. , vol.74 , pp. 234-238
    • Crook, E.M.1    Mathias, A.P.2    Rabin, B.R.3
  • 13
    • 0028836042 scopus 로고
    • Inactivation during denaturation of ribonuclease A by guanidium chloride is accompanied by unfolding at the active site
    • Yang, H.J. and Tsou, C.L. (1995) Inactivation during denaturation of ribonuclease A by guanidium chloride is accompanied by unfolding at the active site. Biochem. J. 305, 379-384
    • (1995) Biochem. J. , vol.305 , pp. 379-384
    • Yang, H.J.1    Tsou, C.L.2
  • 14
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A. and Weinstein, D. (1976) Assay of proteins in the presence of interfering materials. Anal Biochem. 70, 241-250
    • (1976) Anal Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0019888281 scopus 로고
    • Stabilization of proteins by sucrose
    • Lee, J.C. and Timasheff, S.N. (1981) Stabilization of proteins by sucrose. J. Biol. Chem. 256, 7193-7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 18
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T. and Timasheff, S.N. (1982) Stabilization of protein structure by sugars. Biochemistry 21, 6536-6544
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 19
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. (1987) Proteins as molecular chaperones. Nature 328, 378-379
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 20
    • 0026099981 scopus 로고
    • Glycosylation site-binding protein is not required for N-linked glycoprotein synthesis
    • Noiva, R., Kaplan, H.A., and Lennarz, W.J. (1991) Glycosylation site-binding protein is not required for N-linked glycoprotein synthesis. Proc. Natl. Acad. Sci. USA 88, 1986-1990
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1986-1990
    • Noiva, R.1    Kaplan, H.A.2    Lennarz, W.J.3
  • 21
    • 0027889386 scopus 로고
    • Protein disulfide-isomerase: Role in biosynthesis of secretory proteins
    • Lorimer, G., ed. Academic Press, New York
    • Bulleid, N.J. (1993) Protein disulfide-isomerase: Role in biosynthesis of secretory proteins in Advances in Protein Chemistry (Lorimer, G., ed.) Vol. 44, pp. 125-150, Academic Press, New York
    • (1993) Advances in Protein Chemistry , vol.44 , pp. 125-150
    • Bulleid, N.J.1
  • 22
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2


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