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Volumn 278, Issue 2, 2000, Pages 111-122

Selective organic precipitation/extraction of released N-glycans following large-scale enzymatic deglycosylation of glycoproteins

Author keywords

Endo and peptide N glycosidases; Glycoproteins; N and O linked glycans; Oligosaccharide isolation; Solvent precipitation

Indexed keywords

ACETONE; DESALINATION; GLYCOPROTEINS; MAMMALS; OLIGOSACCHARIDES; PEPTIDES; POLYSACCHARIDES; YEAST;

EID: 0034651589     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.1999.4433     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0017407126 scopus 로고
    • The use of endo-β-N-acetylglucosaminidase in characterizing the structure and function of glycoproteins
    • Trimble R. B., Maley F. M. The use of endo-β-N-acetylglucosaminidase in characterizing the structure and function of glycoproteins. J. Biol. Chem. 252:1977;4409-4412.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4409-4412
    • Trimble, R.B.1    Maley, F.M.2
  • 2
    • 0021277449 scopus 로고
    • Early steps in processing of yeast glycoproteins
    • Esmon B., Esmon P. C., Schekman R. Early steps in processing of yeast glycoproteins. J. Biol. Chem. 259:1984;10322-10327.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10322-10327
    • Esmon, B.1    Esmon, P.C.2    Schekman, R.3
  • 3
    • 0021841684 scopus 로고
    • Amplified expression of Streptomyces endo-β-N-acetylglucosaminidase H in Escherichia coli and characterization of the enzyme product
    • Trumbly R. J., Robbins P. W., Belfort M., Ziegler F. D., Maley F., Trimble R. B. Amplified expression of Streptomyces endo-β-N-acetylglucosaminidase H in Escherichia coli and characterization of the enzyme product. J. Biol. Chem. 260:1985;5683-5690.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5683-5690
    • Trumbly, R.J.1    Robbins, P.W.2    Belfort, M.3    Ziegler, F.D.4    Maley, F.5    Trimble, R.B.6
  • 4
    • 0024778571 scopus 로고
    • Enzymatic approaches for studying the structure, synthesis and processing of glycoproteins
    • Tarentino A. L., Trimble R. B., Plummer T. H. Jr. Enzymatic approaches for studying the structure, synthesis and processing of glycoproteins. Methods Cell Biol. 32:1989;111-139.
    • (1989) Methods Cell Biol. , vol.32 , pp. 111-139
    • Tarentino, A.L.1    Trimble, R.B.2    Plummer T.H., Jr.3
  • 5
    • 0026020091 scopus 로고
    • 1 and endo H hydrolyze only high-mannose and hybrid glycans
    • 1 and endo H hydrolyze only high-mannose and hybrid glycans. J. Biol. Chem. 266:1991;1646-1651.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1646-1651
    • Trimble, R.B.1    Tarentino, A.L.2
  • 6
    • 0019218735 scopus 로고
    • Characterization of large oligosaccharide-lipids synthesized in vitro by microsomes from Saccharomyces cerevisiae
    • Trimble R. B., Maley F., Tarentino A. L. Characterization of large oligosaccharide-lipids synthesized in vitro by microsomes from Saccharomyces cerevisiae. J. Biol. Chem. 255:1980;10232-10238.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10232-10238
    • Trimble, R.B.1    Maley, F.2    Tarentino, A.L.3
  • 8
    • 0016710712 scopus 로고
    • Yeast manno-protein biosynthesis: Solubilization and selective assay of four mannosyltransferases
    • Nakajima T., Ballou C. E. Yeast manno-protein biosynthesis: solubilization and selective assay of four mannosyltransferases. Proc. Natl. Acad. Sci. USA. 72:1975;3912-3916.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3912-3916
    • Nakajima, T.1    Ballou, C.E.2
  • 10
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M., Gilles K. A., Hamilton J. K., Rebers P. A., Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 28:1956;350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 11
    • 0018085511 scopus 로고
    • Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay
    • Bearden J. C. Jr. Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay. Biochim. Biophys. Acta. 533:1978;525-529.
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 525-529
    • Bearden J.C., Jr.1
  • 12
    • 0018246098 scopus 로고
    • The effect of carbohydrate depletion on the properties of yeast external invertase
    • Chu F. K., Trimble R. B., Maley F. The effect of carbohydrate depletion on the properties of yeast external invertase. Biochemistry. 253:1978;8691-8693.
    • (1978) Biochemistry , vol.253 , pp. 8691-8693
    • Chu, F.K.1    Trimble, R.B.2    Maley, F.3
  • 13
    • 0016414490 scopus 로고
    • β-d-Fructoside fructohydrolase from yeast
    • Goldstein A., Lampen J. O. β-d-Fructoside fructohydrolase from yeast. Methods Enzymol. 42:1975;504-511.
    • (1975) Methods Enzymol. , vol.42 , pp. 504-511
    • Goldstein, A.1    Lampen, J.O.2
  • 14
    • 0033008023 scopus 로고    scopus 로고
    • 9GlcNAc N-linked oligosaccharide isomers; Role of the Golgi GMA12 galactosyltransferase in core glycan galactosylation
    • 9GlcNAc N-linked oligosaccharide isomers; role of the Golgi GMA12 galactosyltransferase in core glycan galactosylation. Glycobiology. 9:1999;497-505.
    • (1999) Glycobiology , vol.9 , pp. 497-505
    • Ziegler, F.D.1    Cavanagh, J.2    Lubowski, C.3    Trimble, R.B.4
  • 15
    • 0017177631 scopus 로고
    • Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation
    • Skoza L., Kohos S. Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation. Biochem. J. 159:1976;457-462.
    • (1976) Biochem. J. , vol.159 , pp. 457-462
    • Skoza, L.1    Kohos, S.2
  • 16
    • 73049171244 scopus 로고
    • Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids
    • Aminoff D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem. J. 81:1961;384-392.
    • (1961) Biochem. J. , vol.81 , pp. 384-392
    • Aminoff, D.1
  • 17
    • 0024039897 scopus 로고
    • Removal of dodecyl sulfate from protein solution
    • Suzuki H., Terada T. Removal of dodecyl sulfate from protein solution. Anal. Biochem. 172:1988;259-263.
    • (1988) Anal. Biochem. , vol.172 , pp. 259-263
    • Suzuki, H.1    Terada, T.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227:1970;680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0025226048 scopus 로고
    • Structural characterization of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blots
    • Haselbeck A., Schickaneder E., von der Eltz H., Hösel W. Structural characterization of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blots. Anal. Biochem. 191:1990;25-30.
    • (1990) Anal. Biochem. , vol.191 , pp. 25-30
    • Haselbeck, A.1    Schickaneder, E.2    Von Der Eltz, H.3    Hösel, W.4
  • 20
    • 0019258624 scopus 로고
    • Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes
    • Hager D. A., Burgess R. R. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem. 109:1980;76-86.
    • (1980) Anal. Biochem. , vol.109 , pp. 76-86
    • Hager, D.A.1    Burgess, R.R.2
  • 21
    • 0025249194 scopus 로고
    • Amino acid analysis
    • Ozols J. Amino acid analysis. Methods Enzymol. 182:1990;587-601.
    • (1990) Methods Enzymol. , vol.182 , pp. 587-601
    • Ozols, J.1
  • 22
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:1985;631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 23
    • 0014962535 scopus 로고
    • Studies on the oligosaccharide sequence of ribonuclease B
    • Tarentino A. L., Plummer T. H. Jr., Maley F. Studies on the oligosaccharide sequence of ribonuclease B. J. Biol. Chem. 245:1970;4150-4157.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4150-4157
    • Tarentino, A.L.1    Plummer T.H., Jr.2    Maley, F.3
  • 24
    • 0019035061 scopus 로고
    • Structural study of the carbohydrate moiety of bovine pancreatic ribonuclease B
    • Liang C. J., Yamashita K., Kobata A. Structural study of the carbohydrate moiety of bovine pancreatic ribonuclease B. J. Biochem. 88:1980;51-58.
    • (1980) J. Biochem. , vol.88 , pp. 51-58
    • Liang, C.J.1    Yamashita, K.2    Kobata, A.3
  • 25
    • 0015330032 scopus 로고
    • Microheterogeneity and paucidispersity of glycoproteins. II. The carbohydrate of ovalbumin from different species
    • Huang C. C., Montgomery R. D. Microheterogeneity and paucidispersity of glycoproteins. II. The carbohydrate of ovalbumin from different species. Carbohydr. Res. 22:1972;83-89.
    • (1972) Carbohydr. Res. , vol.22 , pp. 83-89
    • Huang, C.C.1    Montgomery, R.D.2
  • 26
    • 0014052337 scopus 로고
    • Purification and properties of yeast invertase
    • Neumann N. P., Lampen J. O. Purification and properties of yeast invertase. Biochemistry. 6:1967;468-475.
    • (1967) Biochemistry , vol.6 , pp. 468-475
    • Neumann, N.P.1    Lampen, J.O.2
  • 27
    • 0023891933 scopus 로고
    • Characterization of the glycosylation sites in yeast external invertase. I. N-linked oligosaccharide content on individual sequons
    • Reddy V. A., Johnson R. S., Biemann K., Williams R. S., Ziegler F. D., Trimble R. B., Maley F. Characterization of the glycosylation sites in yeast external invertase. I. N-linked oligosaccharide content on individual sequons. J. Biol. Chem. 263:1988;6978-6985.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6978-6985
    • Reddy, V.A.1    Johnson, R.S.2    Biemann, K.3    Williams, R.S.4    Ziegler, F.D.5    Trimble, R.B.6    Maley, F.7
  • 28
    • 0023893137 scopus 로고
    • Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo H-resistant sequons
    • Ziegler F. D., Maley F., Trimble R. B. Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo H-resistant sequons. J. Biol. Chem. 263:1988;6986-6992.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6986-6992
    • Ziegler, F.D.1    Maley, F.2    Trimble, R.B.3
  • 29
    • 0032911016 scopus 로고    scopus 로고
    • Determination of N-linked glycosylation of yeast external invertase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Zeng C., Biemann K. Determination of N-linked glycosylation of yeast external invertase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 34:1999;311-329.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 311-329
    • Zeng, C.1    Biemann, K.2
  • 30
    • 0025343453 scopus 로고
    • Localization of α1 → 3-linked mannoses in the N-linked oligosaccharides of Saccharomyces cerevisiae mnn mutants
    • Alvarado E., Ballou L., Hernandez L. M., Ballou C. E. Localization of α1 → 3-linked mannoses in the N-linked oligosaccharides of Saccharomyces cerevisiae mnn mutants. Biochemistry. 29:1990;2471-2482.
    • (1990) Biochemistry , vol.29 , pp. 2471-2482
    • Alvarado, E.1    Ballou, L.2    Hernandez, L.M.3    Ballou, C.E.4
  • 31
    • 0027174395 scopus 로고
    • Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. I. Role of glucose in the initial glycosylation of invertase in the endoplasmic reticulum
    • Verostek M. F., Atkinson P. H., Trimble R. B. Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. I. Role of glucose in the initial glycosylation of invertase in the endoplasmic reticulum. J. Biol. Chem. 268:1993;12095-12103.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12095-12103
    • Verostek, M.F.1    Atkinson, P.H.2    Trimble, R.B.3
  • 34
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics A., Orlean P. Glycoprotein biosynthesis in yeast. FASEB J. 7:1993;540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 35
    • 84998369642 scopus 로고
    • Glycoprotein oligosaccharide synthesis and processing in yeast
    • Trimble R. B., Verostek M. F. Glycoprotein oligosaccharide synthesis and processing in yeast. Trends Glycosci. Glycotechnol. 1:1995;1-30.
    • (1995) Trends Glycosci. Glycotechnol. , vol.1 , pp. 1-30
    • Trimble, R.B.1    Verostek, M.F.2
  • 36
    • 0015522754 scopus 로고
    • Studies on the carbohydrate units of thyroglobulin: Evaluation of their microheterogeneity in the human and calf proteins
    • Arima T., Spiro R. G., Spiro M. J. Studies on the carbohydrate units of thyroglobulin: Evaluation of their microheterogeneity in the human and calf proteins. J. Biol. Chem. 247:1972;1825-1835.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1825-1835
    • Arima, T.1    Spiro, R.G.2    Spiro, M.J.3
  • 37
    • 0015522701 scopus 로고
    • Studies on the carbohydrate units of thyroglobulin: Structure of the mannose-N-acetylglucosamine unit (unit A) of the human and calf proteins
    • Arima T., Spiro R.G. Studies on the carbohydrate units of thyroglobulin: Structure of the mannose-N-acetylglucosamine unit (unit A) of the human and calf proteins. J. Biol. Chem. 247:1972;1836-1848.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1836-1848
    • Arima, T.1    Spiro, R.G.2
  • 38
    • 0017684280 scopus 로고
    • Structure of a carbohydrate moiety of a unit A glycopeotide of calf thyroglobulin
    • Ito S., Yamashita K., Spiro R. G., Kobata A. Structure of a carbohydrate moiety of a unit A glycopeotide of calf thyroglobulin. J. Biochem. 81:1977;1621-1631.
    • (1977) J. Biochem. , vol.81 , pp. 1621-1631
    • Ito, S.1    Yamashita, K.2    Spiro, R.G.3    Kobata, A.4
  • 39
    • 0019580819 scopus 로고
    • The structure of carbohydrate unit B of porcine thyroglobulin
    • Yamamoto K., Tsuji T., Irimura T., Osawa T. The structure of carbohydrate unit B of porcine thyroglobulin. Biochem. J. 195:1981;701-713.
    • (1981) Biochem. J. , vol.195 , pp. 701-713
    • Yamamoto, K.1    Tsuji, T.2    Irimura, T.3    Osawa, T.4
  • 40
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • Spiro R. G., Bhoyroo V. D. Structure of the O-glycosidically linked carbohydrate units of fetuin. J. Biol. Chem. 249:1974;5704-5717.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 41
    • 0005917528 scopus 로고
    • Studies on fetuin, a glycoprotein of fetal serum
    • Spiro R. G. Studies on fetuin, a glycoprotein of fetal serum. J. Biol. Chem. 237:1962;382-388.
    • (1962) J. Biol. Chem. , vol.237 , pp. 382-388
    • Spiro, R.G.1
  • 42
    • 77957231504 scopus 로고
    • Biosynthesis of the O-glycans of the N-acetylgalactosamine-α-Ser/Thr linkage type
    • (Montreuil, J., Vliegenthart, J. F. G., and Schachter, H., Eds.), Elsevier, NY
    • Brockhausen, I.1995 Biosynthesis of the O-glycans of the N-acetylgalactosamine-α-Ser/Thr linkage type. in New Comprehensive Biochemistry (Montreuil, J., Vliegenthart, J. F. G., and Schachter, H., Eds.), Vol. 29a, pp. 201-259, Elsevier, NY.
    • (1995) In New Comprehensive Biochemistry , vol.29 A , pp. 201-259
    • Brockhausen, I.1
  • 43
    • 0028783621 scopus 로고
    • Differences in the glycosylation of recombinant and native human milk bile salt-stimulated lipase revealed by peptide mapping
    • Strömqvist M., Lindgren K., Hansson L., Juneblad K. Differences in the glycosylation of recombinant and native human milk bile salt-stimulated lipase revealed by peptide mapping. J. Chromatogr. A. 718:1995;53-58.
    • (1995) J. Chromatogr. a , vol.718 , pp. 53-58
    • Strömqvist, M.1    Lindgren, K.2    Hansson, L.3    Juneblad, K.4


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