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Volumn 253, Issue 3, 1998, Pages 560-575

Identification of Manα1-3Manα1-2Man and Man-linked phosphate on O- mannosylated recombinant leech-derived tryptase inhibitor produced by Saccharomyces cerevisiae and determination of the solution conformation of the mannosylated polypeptide

Author keywords

Matrix assisted laser desorption ionization mass spectrometry; NMR; O mannosylation; Phosphorylated mannose; Yeast

Indexed keywords

ENZYME INHIBITOR; GLYCINE; MANNOSE; OLIGOSACCHARIDE; POLYPEPTIDE; SERINE; THREONINE; TRYPTASE; TRYPTASE INHIBITOR; TYROSINE; UNCLASSIFIED DRUG; VALINE; LEECH DERIVED TRYPTASE INHIBITOR C; LEECH-DERIVED TRYPTASE INHIBITOR C; OLIGOPEPTIDE; PEPTIDE FRAGMENT; PROTEIN; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR;

EID: 0032056345     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530560.x     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0019888627 scopus 로고
    • Tryptase from human pulmonary mast cells
    • Schwartz, L. B., Lewis, R. A. & Austen, K. F. (1981) Tryptase from human pulmonary mast cells, J. Biol. Chem. 256, 11 939-11 943.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 3
    • 0028520933 scopus 로고
    • A kazal-type inhibitor of human mast cell tryptase - Isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis
    • Sommerhoff, C. P., Sollner, C., Mentele, R., Piechottka, G. P., Auerswald, E. A. & Fritz, H. (1994) A kazal-type inhibitor of human mast cell tryptase - isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis, Biol. Chem. Hoppe-Seyler 375, 685-694.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 685-694
    • Sommerhoff, C.P.1    Sollner, C.2    Mentele, R.3    Piechottka, G.P.4    Auerswald, E.A.5    Fritz, H.6
  • 4
    • 0028520660 scopus 로고
    • Recombinant leech-derived tryptase inhibitor - Construction, production, protein chemical characterization and inhibition of HIV-1 replication
    • Auerswald, E. A., Morenweiser, R., Sommerhoff, C. P., Piechottka, G. P., Eckerskorn, C., Gurtler, L. G. & Fritz, H. (1994) Recombinant leech-derived tryptase inhibitor - construction, production, protein chemical characterization and inhibition of HIV-1 replication, Biol Chem. Hoppe-Seyler 375, 695-703.
    • (1994) Biol Chem. Hoppe-Seyler , vol.375 , pp. 695-703
    • Auerswald, E.A.1    Morenweiser, R.2    Sommerhoff, C.P.3    Piechottka, G.P.4    Eckerskorn, C.5    Gurtler, L.G.6    Fritz, H.7
  • 5
    • 0025963062 scopus 로고
    • Analysis of glycoproteins from Saccharomyces cerevisiae
    • Orlean, P., Kuranda, M. J. & Albright, C. F. (1991) Analysis of glycoproteins from Saccharomyces cerevisiae, Methods Enzymol. 194, 682-697.
    • (1991) Methods Enzymol. , vol.194 , pp. 682-697
    • Orlean, P.1    Kuranda, M.J.2    Albright, C.F.3
  • 6
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A. & Orlean, P. (1993) Glycoprotein biosynthesis in yeast, FASEB J. 7, 540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 8
    • 0029998104 scopus 로고    scopus 로고
    • Purification, characterization and biological evaluation of recombinant leech-derived tryptase inhibitor (rLDTI) expressed at high level in the yeast Saccharomyces cerevisiae
    • Pohlig, G., Fendrich, G., Knecht, R., Eder, B., Piechottka, G., Sommerhoff, C. P. & Heim, J. (1996) Purification, characterization and biological evaluation of recombinant leech-derived tryptase inhibitor (rLDTI) expressed at high level in the yeast Saccharomyces cerevisiae, Eur. J. Biochem. 241, 619-626.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 619-626
    • Pohlig, G.1    Fendrich, G.2    Knecht, R.3    Eder, B.4    Piechottka, G.5    Sommerhoff, C.P.6    Heim, J.7
  • 9
    • 0028152841 scopus 로고
    • C-terminal proteolytic degradation of recombinant desulfato-hirudin and its mutants in the yeast Saccharomyces cerevisiae
    • Heim, J., Takabyashi, K., Meyhack, B., Märki, W. & Pohlig, G. (1994) C-terminal proteolytic degradation of recombinant desulfato-hirudin and its mutants in the yeast Saccharomyces cerevisiae, Eur. J. Biochem. 226, 341-353.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 341-353
    • Heim, J.1    Takabyashi, K.2    Meyhack, B.3    Märki, W.4    Pohlig, G.5
  • 10
    • 0024513452 scopus 로고
    • O-mannosylation of recombinant human insulin-like growth factor I (IGF-I) produced in Saccharomyces cerevisiae
    • Hård, K., Bitter, W., Kamerling, J. P. & Vliegenthart, J. F. G. (1989) O-mannosylation of recombinant human insulin-like growth factor I (IGF-I) produced in Saccharomyces cerevisiae, FEBS Lett. 248, 111-114.
    • (1989) FEBS Lett. , vol.248 , pp. 111-114
    • Hård, K.1    Bitter, W.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 11
    • 0002540814 scopus 로고
    • Compositional analysis of glycoproteins
    • Fukuda, M. & Kobata, A., eds IRL press, Oxford
    • Manzi, A. E. & Varki, A. (1993) Compositional analysis of glycoproteins, in Glycobiology, a pratical approach (Fukuda, M. & Kobata, A., eds) pp. 27-78, IRL press, Oxford.
    • (1993) Glycobiology, a Pratical Approach , pp. 27-78
    • Manzi, A.E.1    Varki, A.2
  • 12
    • 0343373375 scopus 로고
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins, Adv. Carbohydr. Chem. Biochem. 41, 209-374.
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 209-374
    • Vliegenthart, J.F.G.1    Dorland, L.2    Van Halbeek, H.3
  • 13
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4593.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4593
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 14
    • 33845378943 scopus 로고
    • Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • Davis, D. G. & Bax, A. (1985) Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy, J. Amm. Chem. Soc. 107, 2820-2820
    • (1985) J. Amm. Chem. Soc. , vol.107 , pp. 2820-2820
    • Davis, D.G.1    Bax, A.2
  • 15
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sørensen, O. W. & Ernst, R. R. (1982) Multiple quantum filters for elucidating NMR coupling networks, J. Am. Chem. Soc. 104, 6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 16
    • 45949127312 scopus 로고
    • P.E.COSY a simple alternative to E.COSY
    • Müller, L. (1987) P.E.COSY a simple alternative to E.COSY, J. Magn. Reson. 72, 191-196.
    • (1987) J. Magn. Reson. , vol.72 , pp. 191-196
    • Müller, L.1
  • 17
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. & Ruben, D. J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy, Chem. Phys. Lett. 69, 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 18
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 20
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel, T. F. (1991) An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance, Prog. Biophys. Mol. Biol. 56, 43-78.
    • (1991) Prog. Biophys. Mol. Biol. , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 22
    • 0001154884 scopus 로고
    • Lability of asparagine and aspartic acid residues in proteins and peptides -spontaneous deamidation and isomerization reactions
    • Ahern, T. J. & Manning, M. C., eds Plenum Press, New York
    • Clarke, S., Stephenson, R. C. & Lowenson, J. D. (1992) Lability of asparagine and aspartic acid residues in proteins and peptides -spontaneous deamidation and isomerization reactions, in Chemical and physical pathways of protein degradation, (A) Stability of protein pharmaceuticals (Ahern, T. J. & Manning, M. C., eds) pp. 1-29, Plenum Press, New York.
    • (1992) Chemical and Physical Pathways of Protein Degradation, (A) Stability of Protein Pharmaceuticals , pp. 1-29
    • Clarke, S.1    Stephenson, R.C.2    Lowenson, J.D.3
  • 23
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol.222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 24
    • 85013548278 scopus 로고
    • Glycosylation of heterologously expressed proteins: Problems and solutions
    • Marshak, D. R. & Darrell, T. L., eds Cold Spring Harbour Press, Cold Spring Harbour
    • Bergh, M. L. E., Hubbard, S. C. & Robbins, P. W. (1988) Glycosylation of heterologously expressed proteins: Problems and solutions, in Therapeutic peptides and proteins: Assessing the new technologies (Marshak, D. R. & Darrell, T. L., eds) vol. 29, pp. 59-67, Cold Spring Harbour Press, Cold Spring Harbour.
    • (1988) Therapeutic Peptides and Proteins: Assessing the New Technologies , vol.29 , pp. 59-67
    • Bergh, M.L.E.1    Hubbard, S.C.2    Robbins, P.W.3
  • 25
    • 0017871265 scopus 로고
    • Antibodies against oligosaccharides coupled to proteins: Characterization of carbohydrate specificity of radioimmune assay
    • Zopf, D. A., Tsai, C.-M. & Ginsburg, V. (1978) Antibodies against oligosaccharides coupled to proteins: characterization of carbohydrate specificity of radioimmune assay, Arch. Biochem. Biophys. 185, 61-71.
    • (1978) Arch. Biochem. Biophys. , vol.185 , pp. 61-71
    • Zopf, D.A.1    Tsai, C.-M.2    Ginsburg, V.3
  • 26
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implications
    • Cumming, D. A. (1991) Glycosylation of recombinant protein therapeutics: control and functional implications, Glycobiology 1, 115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cumming, D.A.1
  • 27
    • 0024348553 scopus 로고
    • Isolation and characterization of a glycosylated form of human insulin-like growth factor I produced in Saccharomyces cerevisiae -Identification of a new motif for O-glycosylation
    • Gellerfors, P., Axelsson, K., Helander, A., Johansson, S., Kenne, L., Lindqvist, S., Pavlu, B., Skottner, A. & Fryklund, L. (1989) Isolation and characterization of a glycosylated form of human insulin-like growth factor I produced in Saccharomyces cerevisiae -Identification of a new motif for O-glycosylation, J. Biol. Chem. 264, 11 444-11 449.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11444-11449
    • Gellerfors, P.1    Axelsson, K.2    Helander, A.3    Johansson, S.4    Kenne, L.5    Lindqvist, S.6    Pavlu, B.7    Skottner, A.8    Fryklund, L.9
  • 31
    • 0028165537 scopus 로고
    • Localization of an O-glycosylated site in the recombinant barley α-amylase 1 produced in yeast and correction of the amino acid sequence using matrix-assisted laser desorption ionization mass spectrometry of peptide mixtures
    • Andersen, J. S., Søgaard, M., Svensson, B. & Roepstorff, P. (1994) Localization of an O-glycosylated site in the recombinant barley α-amylase 1 produced in yeast and correction of the amino acid sequence using matrix-assisted laser desorption ionization mass spectrometry of peptide mixtures, Biol. Mass Spectrom. 23, 547-554.
    • (1994) Biol. Mass Spectrom. , vol.23 , pp. 547-554
    • Andersen, J.S.1    Søgaard, M.2    Svensson, B.3    Roepstorff, P.4
  • 32
    • 0029035781 scopus 로고
    • Glycan modification of a thermostable recombinant (1-3,1-4)-β-glucanase secreted from Saccharomyces cerevisiae is determined by strain and culture conditions
    • Meldgaard, M., Harthill, J., Petersen, B. & Olsen, O. (1995) Glycan modification of a thermostable recombinant (1-3,1-4)-β-glucanase secreted from Saccharomyces cerevisiae is determined by strain and culture conditions, Glycoconjugate J. 12, 380-390.
    • (1995) Glycoconjugate J. , vol.12 , pp. 380-390
    • Meldgaard, M.1    Harthill, J.2    Petersen, B.3    Olsen, O.4
  • 33
    • 0028793842 scopus 로고
    • N- and O-glycosylation and phosphorylation of the bar secretion leader derived from the barrier protease of Saccharomyces cerevisiae
    • Jars, M. U., Osborn, S., Forstrom, J. & MacKay, V. L. (1995) N- and O-glycosylation and phosphorylation of the bar secretion leader derived from the barrier protease of Saccharomyces cerevisiae, J. Biol. Chem. 270, 24 810-24 817.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24810-24817
    • Jars, M.U.1    Osborn, S.2    Forstrom, J.3    MacKay, V.L.4
  • 34
    • 0025973305 scopus 로고
    • Protein O-glycosylation in Saccharomyces cerevisiae - Purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase
    • Strahl-Bolsinger, S. & Tanner, W. (1991) Protein O-glycosylation in Saccharomyces cerevisiae - purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase, Eur. J. Biochem. 196, 185-190.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 185-190
    • Strahl-Bolsinger, S.1    Tanner, W.2


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