메뉴 건너뛰기




Volumn 1480, Issue 1-2, 2000, Pages 222-234

Active site studies of bovine α1→3-galactosyltransferase and its secondary structure prediction

Author keywords

1 3 Galactosyltransferase; Fourier transform infrared spectroscopy; Glycosyltransferase

Indexed keywords

DISACCHARIDE; GALACTOSYLTRANSFERASE; GLYCOSYLTRANSFERASE; MONOSACCHARIDE;

EID: 0034647861     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00074-1     Document Type: Article
Times cited : (12)

References (54)
  • 1
    • 0025254311 scopus 로고
    • Bovine beta 1-4-galactosyltransferase: Two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins
    • Russo R.N., Shaper N.L., Shaper J.H. Bovine beta 1-4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins. J. Biol. Chem. 265:1990;3324-3331.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3324-3331
    • Russo, R.N.1    Shaper, N.L.2    Shaper, J.H.3
  • 2
    • 0024441285 scopus 로고
    • Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells
    • Masibay A.S., Qasba P.K. Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells. Proc. Natl. Acad. Sci. USA. 86:1989;5733-5737.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5733-5737
    • Masibay, A.S.1    Qasba, P.K.2
  • 3
    • 0024312590 scopus 로고
    • Cloning of cDNA encoding the membrane-bound form of bovine beta-1,4-galactosyltransferase
    • D'Agostaro G., Bendiak B., Tropak M. Cloning of cDNA encoding the membrane-bound form of bovine beta-1,4-galactosyltransferase. Eur. J. Biochem. 183:1989;211-217.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 211-217
    • D'Agostaro, G.1    Bendiak, B.2    Tropak, M.3
  • 4
    • 0345009059 scopus 로고
    • Bovine galactosyltransferase: Identification of a clone by direct immunological screening of a cDNA expression library
    • Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F. Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library. Proc. Natl. Acad. Sci. USA. 83:1986;1573-1577.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1573-1577
    • Shaper, N.L.1    Shaper, J.H.2    Meuth, J.L.3    Fox, J.L.4    Chang, H.5    Kirsch, I.R.6    Hollis, G.F.7
  • 5
    • 0022542290 scopus 로고
    • Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase
    • Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K. Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase. Proc. Natl. Acad. Sci. USA. 83:1986;4720-4724.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4720-4724
    • Narimatsu, H.1    Sinha, S.2    Brew, K.3    Okayama, H.4    Qasba, P.K.5
  • 6
    • 0024310039 scopus 로고
    • Bovine alpha-1,3-galactosyltransferase: Isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA
    • Joziasse D.H., Shaper J.H., Van den Eijnden D.H., Van Tunen A.J., Shaper N.L. Bovine alpha-1,3-galactosyltransferase: isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA. J. Biol. Chem. 264:1989;14290-14297.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14290-14297
    • Joziasse, D.H.1    Shaper, J.H.2    Van Den Eijnden, D.H.3    Van Tunen, A.J.4    Shaper, N.L.5
  • 7
    • 0028230361 scopus 로고
    • Defining the minimal size of catalytically active primate alpha 1,3 galactosyltransferase structure-function studies on the recombinant truncated enzyme
    • Henion T.R., Macher B.A., Anaraki F., Galili U. Defining the minimal size of catalytically active primate alpha 1,3 galactosyltransferase structure-function studies on the recombinant truncated enzyme. Glycobiology. 4:1994;193-201.
    • (1994) Glycobiology , vol.4 , pp. 193-201
    • Henion, T.R.1    Macher, B.A.2    Anaraki, F.3    Galili, U.4
  • 9
    • 0015239690 scopus 로고
    • Studies on galactosyltransferase. Kinetic investigations with N-acetylglucosamine as the galactosyl group acceptor
    • Morrison J.F., Ebner K.E. Studies on galactosyltransferase. Kinetic investigations with N-acetylglucosamine as the galactosyl group acceptor. J. Biol. Chem. 246:1971;3977-3984.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3977-3984
    • Morrison, J.F.1    Ebner, K.E.2
  • 10
    • 0015239690 scopus 로고
    • Studies on Galactosyltransferase. Kinetic investigations with glucose as the galactosyl group acceptor
    • Morrison J.F., Ebner K.E. Studies on Galactosyltransferase. Kinetic investigations with glucose as the galactosyl group acceptor. J. Biol. Chem. 246:1971;3985-3991.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3985-3991
    • Morrison, J.F.1    Ebner, K.E.2
  • 11
    • 0021271447 scopus 로고
    • The lactose synthase acceptor site: A structural map derived from acceptor studies
    • Berliner L.J., Davis M.E., Ebner K.E., Beyer T.A., Bell J.E. The lactose synthase acceptor site: a structural map derived from acceptor studies. Mol. Cell Biochem. 62:1984;37-42.
    • (1984) Mol. Cell Biochem. , vol.62 , pp. 37-42
    • Berliner, L.J.1    Davis, M.E.2    Ebner, K.E.3    Beyer, T.A.4    Bell, J.E.5
  • 12
    • 0025971614 scopus 로고
    • Flexibility in the donor substrate specificity of beta 1,4-galactosyltransferase application in the synthesis of complex carbohydrates
    • Palcic M.M., Hindsgaul O. Flexibility in the donor substrate specificity of beta 1,4-galactosyltransferase application in the synthesis of complex carbohydrates. Glycobiology. 1:1991;205-209.
    • (1991) Glycobiology , vol.1 , pp. 205-209
    • Palcic, M.M.1    Hindsgaul, O.2
  • 13
    • 0014198092 scopus 로고
    • The isolation and identification of the B protein of lactose synthetase as alpha-lactalbumin
    • Brodbeck U., Denton W.L., Tanahashi N., Ebner K.E. The isolation and identification of the B protein of lactose synthetase as alpha-lactalbumin. J. Biol. Chem. 242:1967;1391-1397.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1391-1397
    • Brodbeck, U.1    Denton, W.L.2    Tanahashi, N.3    Ebner, K.E.4
  • 14
    • 0014251737 scopus 로고
    • The role of alpha-lactalbumin and the A protein in lactose synthetase: A unique mechanism for the control of a biological reaction
    • Brew K., Vanaman T.C., Hill R.L. The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Proc. Natl. Acad. Sci. USA. 59:1967;491-497.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.59 , pp. 491-497
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 15
    • 0030800608 scopus 로고    scopus 로고
    • Molecular divergence of lysozymes and alpha-lactalbumin
    • Qasba P.K., Kumar S. Molecular divergence of lysozymes and alpha-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 32:1997;255-306.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 255-306
    • Qasba, P.K.1    Kumar, S.2
  • 16
    • 0022350361 scopus 로고
    • Biosynthesis of terminal Gal-alpha1-3Gal-beta1-4GlcNAc-R oligosaccharide sequences on glycoconjugates
    • Blanken W.M., Van den Eijnden D.H. Biosynthesis of terminal Gal-alpha1-3Gal-beta1-4GlcNAc-R oligosaccharide sequences on glycoconjugates. J. Biol. Chem. 260:1985;12927-12934.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12927-12934
    • Blanken, W.M.1    Van Den Eijnden, D.H.2
  • 17
    • 0031398997 scopus 로고    scopus 로고
    • Acceptor hydroxyl group mapping for calf thymus alpha-(1-3)-galactosyltransferase and enzymatic synthesis of alpha-D-Galp-(1-3)-beta-D-Galp-(1-4)-beta-D-GlcpNAc analogs
    • Sujino K., Malet C., Hindsgaul O., Palcic M.M. Acceptor hydroxyl group mapping for calf thymus alpha-(1-3)-galactosyltransferase and enzymatic synthesis of alpha-D-Galp-(1-3)-beta-D-Galp-(1-4)-beta-D-GlcpNAc analogs. Carbohydr. Res. 305:1998;483-489.
    • (1998) Carbohydr. Res. , vol.305 , pp. 483-489
    • Sujino, K.1    Malet, C.2    Hindsgaul, O.3    Palcic, M.M.4
  • 19
    • 0032800234 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of alpha1,3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides
    • Stults C.L.M., Macher B.A., Bhatti R., Srivastava O.P., Hindsgaul O. Characterization of the substrate specificity of alpha1,3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides. Glycobiology. 9:1999;661-668.
    • (1999) Glycobiology , vol.9 , pp. 661-668
    • Stults, C.L.M.1    Macher, B.A.2    Bhatti, R.3    Srivastava, O.P.4    Hindsgaul, O.5
  • 20
    • 0033105724 scopus 로고    scopus 로고
    • Purification and characterization of an alpha-galactosyltransferase from Trypanosoma brucei
    • Pingel S., Rheinweiler U., Kolb V., Duszenko M. Purification and characterization of an alpha-galactosyltransferase from Trypanosoma brucei. Biochem. J. 338:1999;545-551.
    • (1999) Biochem. J. , vol.338 , pp. 545-551
    • Pingel, S.1    Rheinweiler, U.2    Kolb, V.3    Duszenko, M.4
  • 21
    • 0025042557 scopus 로고
    • Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling
    • Yadav S., Brew K. Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling. J. Biol. Chem. 265:1990;14163-14169.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14163-14169
    • Yadav, S.1    Brew, K.2
  • 22
    • 0024297335 scopus 로고
    • Man, apes, and old world monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells
    • Galili U., Shohet S.B., Kobrin E., Stults C.L.M., Macher B.A. Man, apes, and old world monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells. J. Biol. Chem. 263:1988;17755-17762.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17755-17762
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3    Stults, C.L.M.4    Macher, B.A.5
  • 23
    • 0025264624 scopus 로고
    • Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase cDNA
    • Larsen R.D., Rivera-Marrero C.A., Ernst L.K., Cummings R.D., Lowe J.B. Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase cDNA. J. Biol. Chem. 265:1990;7055-7061.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7055-7061
    • Larsen, R.D.1    Rivera-Marrero, C.A.2    Ernst, L.K.3    Cummings, R.D.4    Lowe, J.B.5
  • 24
    • 0025895390 scopus 로고
    • Characterization of an alpha1-3-galactosyltransferase homologue on human chromosome 12 that is organized as a processed pseudogene
    • Joziasse D.H., Shaper J.H., Jabs E.W., Shaper N.L. Characterization of an alpha1-3-galactosyltransferase homologue on human chromosome 12 that is organized as a processed pseudogene. J. Biol. Chem. 266:1991;6991-6998.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6991-6998
    • Joziasse, D.H.1    Shaper, J.H.2    Jabs, E.W.3    Shaper, N.L.4
  • 25
    • 0028171342 scopus 로고
    • Oligosaccharides and discordant xenotransplantation
    • Cooper D.K., Koren E., Oriol R. Oligosaccharides and discordant xenotransplantation. Immunol. Rev. 141:1994;31-58.
    • (1994) Immunol. Rev. , vol.141 , pp. 31-58
    • Cooper, D.K.1    Koren, E.2    Oriol, R.3
  • 26
    • 0023950850 scopus 로고
    • Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora
    • Galili U., Mandrell R.E., Hamadeh R.M., Shohet S.B., Griffiss J.M. Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora. Infect. Immun. 56:1988;1730-1737.
    • (1988) Infect. Immun. , vol.56 , pp. 1730-1737
    • Galili, U.1    Mandrell, R.E.2    Hamadeh, R.M.3    Shohet, S.B.4    Griffiss, J.M.5
  • 27
    • 0032528232 scopus 로고    scopus 로고
    • Highly efficient chemoenzymatic synthesis of alpha-galactosyl epitopes with a recombinant alpha(1-3)-galactosyltransferase
    • Fang J., Li J., Chen X., Zhang Y., Wang J., Guo Z., Zhang W., Yu L., Brew K., Wang P.G. Highly efficient chemoenzymatic synthesis of alpha-galactosyl epitopes with a recombinant alpha(1-3)-galactosyltransferase. J. Am. Chem. Soc. 120:1998;6635-6638.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6635-6638
    • Fang, J.1    Li, J.2    Chen, X.3    Zhang, Y.4    Wang, J.5    Guo, Z.6    Zhang, W.7    Yu, L.8    Brew, K.9    Wang, P.G.10
  • 29
    • 0027522253 scopus 로고
    • Expression of deletion constructs of bovine beta-1,4-galactosyltransferase in Escherichia coli: Importance of Cys134 for its activity
    • Boeggeman E.E., Balaji P.V., Sethi N., Masibay A.S., Qasba P.K. Expression of deletion constructs of bovine beta-1,4-galactosyltransferase in Escherichia coli: importance of Cys134 for its activity. Protein Eng. 6:1993;779-785.
    • (1993) Protein Eng. , vol.6 , pp. 779-785
    • Boeggeman, E.E.1    Balaji, P.V.2    Sethi, N.3    Masibay, A.S.4    Qasba, P.K.5
  • 30
    • 0029619173 scopus 로고
    • Functional domains of bovine beta-1,4 galactosyltransferase
    • Boeggeman E.E., Balaji P.V., Qasba P.K. Functional domains of bovine beta-1,4 galactosyltransferase. Glycoconjug. J. 12:1995;865-878.
    • (1995) Glycoconjug. J. , vol.12 , pp. 865-878
    • Boeggeman, E.E.1    Balaji, P.V.2    Qasba, P.K.3
  • 31
    • 0030922424 scopus 로고    scopus 로고
    • Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
    • Seto N.O., Palcic M.M., Compston C.A., Li H., Bundle D.R., Narang S.A. Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J. Biol. Chem. 272:1997;14133-14138.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14133-14138
    • Seto, N.O.1    Palcic, M.M.2    Compston, C.A.3    Li, H.4    Bundle, D.R.5    Narang, S.A.6
  • 32
    • 0033083847 scopus 로고    scopus 로고
    • Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli
    • Seto N.O., Compston C.A., Evans S.V., Bundle D.R., Narang S.A., Palcic M.M. Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. Eur. J. Biochem. 259:1999;770-775.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 770-775
    • Seto, N.O.1    Compston, C.A.2    Evans, S.V.3    Bundle, D.R.4    Narang, S.A.5    Palcic, M.M.6
  • 33
    • 0031150139 scopus 로고    scopus 로고
    • -1 range and quantitative infrared spectroscopy of aqueous solutions
    • -1 range and quantitative infrared spectroscopy of aqueous solutions. Anal. Biochem. 248:1997;234-245.
    • (1997) Anal. Biochem. , vol.248 , pp. 234-245
    • Venyaminov, S.Y.1    Prendergast, F.G.2
  • 34
    • 0024622619 scopus 로고
    • On the spectral subtraction of water from the FTIR spectra of aqueous solutions of proteins
    • Dousseau F., Therrien M., Pezolet M. On the spectral subtraction of water from the FTIR spectra of aqueous solutions of proteins. Appl. Spectrosc. 43:1989;538-542.
    • (1989) Appl. Spectrosc. , vol.43 , pp. 538-542
    • Dousseau, F.1    Therrien, M.2    Pezolet, M.3
  • 35
    • 0002298684 scopus 로고    scopus 로고
    • Protein structural studies using vibrational circular dichroism spectroscopy
    • in: H.A. Havel (Ed.), VCH, New York
    • T.A. Keiderling, Protein structural studies using vibrational circular dichroism spectroscopy, in: H.A. Havel (Ed.), Spectroscopic Methods for determining Protein Structure in Solution, VCH, New York, 1996, pp. 163-189.
    • (1996) Spectroscopic Methods for Determining Protein Structure in Solution , pp. 163-189
    • Keiderling, T.A.1
  • 36
    • 0025734103 scopus 로고
    • Statistical analyses of the vibrational circular dichroism of selected proteins and relationship to secondary structures
    • Pancoska P., Yasui S.C., Keiderling T.A. Statistical analyses of the vibrational circular dichroism of selected proteins and relationship to secondary structures. Biochemistry. 30:1991;5089-5103.
    • (1991) Biochemistry , vol.30 , pp. 5089-5103
    • Pancoska, P.1    Yasui, S.C.2    Keiderling, T.A.3
  • 37
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • Kauppinen J.K., Moffatt D.J., Mantsch H.H., Cameron D.G. Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl. Spectrosc. 35:1981;271-276.
    • (1981) Appl. Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 38
    • 0024821263 scopus 로고
    • Molecular mechanics. The MM3 force field for hydrocarbons. 1
    • Allinger N.L., Yuh Y.H., Lii J.H. Molecular mechanics. The MM3 force field for hydrocarbons. 1. J. Am. Chem. Soc. 111:1989;8551-8556.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8551-8556
    • Allinger, N.L.1    Yuh, Y.H.2    Lii, J.H.3
  • 39
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi H., Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130:1986;290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 40
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz W.K., Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta. 952:1988;115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 41
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy a critical assessment
    • Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy a critical assessment. Biochemistry. 32:1993;389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 42
    • 0026484855 scopus 로고
    • Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlations in Fourier transform infrared spectroscopy
    • Prestrelski S.J., Byler D.M., Liebman M.N. Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlations in Fourier transform infrared spectroscopy. Proteins. 14:1992;440-450.
    • (1992) Proteins , vol.14 , pp. 440-450
    • Prestrelski, S.J.1    Byler, D.M.2    Liebman, M.N.3
  • 43
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo J.L., Muga A., Castresana J., Goni F.M. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:1993;23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 44
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A., Huang P., Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry. 29:1990;3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 46
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and II bands
    • Miyazawa T., Blout E.R. The infrared spectra of polypeptides in various conformations: amide I and II bands. J. Am. Chem. Soc. 83:1961;712-719.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 47
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S., Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein. Chem. 38:1986;181-364.
    • (1986) Adv. Protein. Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 48
    • 0027477526 scopus 로고
    • Structural analysis based on state-space modeling
    • Stultz C.M., White J.V., Smith T.F. Structural analysis based on state-space modeling. Protein Sci. 2:1993;305-314.
    • (1993) Protein Sci. , vol.2 , pp. 305-314
    • Stultz, C.M.1    White, J.V.2    Smith, T.F.3
  • 49
    • 77956716177 scopus 로고    scopus 로고
    • Predicting protein structure with probabilistic models
    • in: N. Allewell, C. Woodward (Eds.), JAI Press, Greenwich
    • C.M. Stultz, R. Nambudripad, R.H. Lathrop, J.V. White, Predicting protein structure with probabilistic models, in: N. Allewell, C. Woodward (Eds.), Advances in Molecular and Cell Biology, JAI Press, Greenwich, 1997, pp. 447-506.
    • (1997) Advances in Molecular and Cell Biology , pp. 447-506
    • Stultz, C.M.1    Nambudripad, R.2    Lathrop, R.H.3    White, J.V.4
  • 50
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino-acid sequences
    • White J.V., Stultz C.M., Smith T.F. Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Math. Biosci. 119:1994;35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3
  • 52
    • 0017159511 scopus 로고
    • Metal ion activation of galactosyltransferase
    • Powell J.T., Brew K. Metal ion activation of galactosyltransferase. J. Biol. Chem. 251:1976;3645-3652.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3645-3652
    • Powell, J.T.1    Brew, K.2
  • 53
    • 0343102548 scopus 로고    scopus 로고
    • High yield expression in E. coli, kinetic characterization and mutagenesis study of UDP-Gal:Galβ1-4GlcNAc α1-3, galactosyltrasferase
    • Abstract # 132, Baltimore, MD
    • Y. Zhang, M. Arana, K. Brew, High yield expression in E. coli, kinetic characterization and mutagenesis study of UDP-Gal:Galβ1-4GlcNAc α1-3, galactosyltrasferase, in: 3rd Annual Conference of the Society for Glycobiology, Abstract # 132, Baltimore, MD, 1998.
    • (1998) In: 3rd Annual Conference of the Society for Glycobiology
    • Zhang, Y.1    Arana, M.2    Brew, K.3
  • 54
    • 0017098758 scopus 로고
    • The kinetic mechansim of bovine milk galactosyltransferase. The role of alpha-lactalbumin
    • Bell J.E., Beyer T.A., Hill R.L. The kinetic mechansim of bovine milk galactosyltransferase. The role of alpha-lactalbumin. J. Biol. Chem. 251:1976;3003-3013.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3003-3013
    • Bell, J.E.1    Beyer, T.A.2    Hill, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.