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Volumn 155, Issue 1, 1996, Pages 23-29

Purification and characterization of the carboxyldomain of human hexokinase type III expressed as fusion protein

Author keywords

D glucose; Fusion protein; Glutathione S transferase; Hexokinase type III; pGEX 2T vector

Indexed keywords

GLUTATHIONE TRANSFERASE; HEXOKINASE; HYBRID PROTEIN; RECOMBINANT PROTEIN;

EID: 0030060318     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00714329     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0002002378 scopus 로고
    • Regulation of mammalian hexokinase activity. in E. Beitner (ed.). Regulation of Carbohydrate Metabolism
    • Wilson JE: Regulation of mammalian hexokinase activity. In E. Beitner (ed.). Regulation of Carbohydrate Metabolism. CRC Press, Boca Raton, FL, 1984, vol I, pp 45-85
    • (1984) CRC Press, Boca Raton, FL , vol.1 , pp. 45-85
    • Wilson, J.E.1
  • 2
    • 0023854041 scopus 로고
    • The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA
    • Schwab DA, Wilson JE: The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA. J Biol Chem 263: 3220-3224, 1988
    • (1988) J Biol Chem , vol.263 , pp. 3220-3224
    • Schwab, D.A.1    Wilson, J.E.2
  • 3
    • 0024202709 scopus 로고
    • Human hexokinase: Sequence of amino- And carboxyl-tenninal halves are homologous
    • Nishi S, Seino S, Bell GI: Human hexokinase: sequence of amino- and carboxyl-tenninal halves are homologous. Biochem Biophys Res Commun 157: 937-943, 1988
    • (1988) Biochem Biophys Res Commun , vol.157 , pp. 937-943
    • Nishi, S.1    Seino, S.2    Bell, G.I.3
  • 5
    • 0024605390 scopus 로고
    • Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase
    • Schwab DA, Wilson JE: Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase. Proc Natl Acad Sci USA 86: 2563-2567, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2563-2567
    • Schwab, D.A.1    Wilson, J.E.2
  • 6
    • 0025218127 scopus 로고
    • Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA enconding a mitochondrial bindable form of hexokinase
    • Arora KK, Fanciulli M, Pedersen L: Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA enconding a mitochondrial bindable form of hexokinase. J Biol Chem 265: 6481-6488, 1990
    • (1990) J Biol Chem , vol.265 , pp. 6481-6488
    • Arora, K.K.1    Fanciulli, M.2    Pedersen, L.3
  • 7
    • 0025905408 scopus 로고
    • Complete amino acid sequence of the type III isozyme of rat hexokinase, deduced from the cloned cDNA
    • Schwab DA, Wilson JE: Complete amino acid sequence of the type III isozyme of rat hexokinase, deduced from the cloned cDNA. Arch Biochem Biophys 285: 365-370, 1991
    • (1991) Arch Biochem Biophys , vol.285 , pp. 365-370
    • Schwab, D.A.1    Wilson, J.E.2
  • 8
    • 0025873080 scopus 로고
    • Complete amino acid sequence of the type II isozyme of rat hexokinase, deduced from the cloned cDNA: Comparison with a hexokinase from Novikoff ascite tumor
    • Thelen AP, Wilson JE: Complete amino acid sequence of the type II isozyme of rat hexokinase, deduced from the cloned cDNA: comparison with a hexokinase from Novikoff ascite tumor. Arch Biochem Biophys 286: 645-651, 1991
    • (1991) Arch Biochem Biophys , vol.286 , pp. 645-651
    • Thelen, A.P.1    Wilson, J.E.2
  • 9
    • 0027440347 scopus 로고
    • Human hexokinase II: Sequence and homology to other hexokinases
    • Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun 197: 98-74, 1993
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 98-174
    • Deeb, S.S.1    Malkki, M.2    Laakso, M.3
  • 10
    • 0023204503 scopus 로고
    • Rat brain hexokinase: Location of the substrate hexose binding site in a structural domain at the C-terminus of the enzyme
    • Schirch DM, Wilson JE: Rat brain hexokinase: location of the substrate hexose binding site in a structural domain at the C-terminus of the enzyme. Arch Biochem Biophys 254: 385-396, 1987
    • (1987) Arch Biochem Biophys , vol.254 , pp. 385-396
    • Schirch, D.M.1    Wilson, J.E.2
  • 11
    • 0023498025 scopus 로고
    • Rat brain hexokinase: Location of the allosteric regulatory site in a structural domain at the N-terminous of the enzyme
    • White TK, Wilson JE: Rat brain hexokinase: location of the allosteric regulatory site in a structural domain at the N-terminous of the enzyme. Arch Biochem Biophys 259: 402-411, 1987
    • (1987) Arch Biochem Biophys , vol.259 , pp. 402-411
    • White, T.K.1    Wilson, J.E.2
  • 12
    • 0024415432 scopus 로고
    • Isolation and characterization of the discrete N- And C-terminal halves of rat brain hexokinase: Retention of full catalytic activity in the isolated C-terminal half
    • White TK, Wilson JE: Isolation and characterization of the discrete N- and C-terminal halves of rat brain hexokinase: retention of full catalytic activity in the isolated C-terminal half. Arch Biochem Biophys 274: 375-393, 1989
    • (1989) Arch Biochem Biophys , vol.274 , pp. 375-393
    • White, T.K.1    Wilson, J.E.2
  • 13
    • 0027166197 scopus 로고
    • Structure/function relationships in hexokinase. Site directed mutational analyses and characterization of overexpressed figments implicate different functions for the N- And C-terminal halves of the enzyme
    • Arora KK, Filburn CR, Pedersen PL: Structure/function relationships in hexokinase. Site directed mutational analyses and characterization of overexpressed figments implicate different functions for the N- and C-terminal halves of the enzyme. J Biol Chem 268: 18259-18266, 1993
    • (1993) J Biol Chem , vol.268 , pp. 18259-18266
    • Arora, K.K.1    Filburn, C.R.2    Pedersen, P.L.3
  • 15
    • 0020524206 scopus 로고
    • Pig red blood cell hexokinase: Evidence for the presence of hexokinase types II and III, and their purification and characterization
    • Stocchi V, Magnani M, Novelli G, Dachà M, Fornaini G: Pig red blood cell hexokinase: evidence for the presence of hexokinase types II and III, and their purification and characterization. Arch Biochem Biophys 226: 365-376, 1983
    • (1983) Arch Biochem Biophys , vol.226 , pp. 365-376
    • Stocchi, V.1    Magnani, M.2    Novelli, G.3    Dachà, M.4    Fornaini, G.5
  • 16
    • 0023090673 scopus 로고
    • Hexokinase isoenzymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C
    • Radojkovic J, Ureta T: Hexokinase isoenzymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C. Biochem J 242: 895-903, 1987
    • (1987) Biochem J , vol.242 , pp. 895-903
    • Radojkovic, J.1    Ureta, T.2
  • 18
    • 0026825710 scopus 로고
    • Preparative purification of pig red blood cell hexokinase type III using a new efficient chromatographic support
    • Stocchi V, Masat L, Biagiarelli B, Piccoli G, Palma F, Cucchiarini L, Dachà M: Preparative purification of pig red blood cell hexokinase type III using a new efficient chromatographic support. Prep Biochem 22: 41-51, 1992
    • (1992) Prep Biochem , vol.22 , pp. 41-51
    • Stocchi, V.1    Masat, L.2    Biagiarelli, B.3    Piccoli, G.4    Palma, F.5    Cucchiarini, L.6    Dachà, M.7
  • 19
    • 0026680847 scopus 로고
    • Localization of the type III isozyme of hexokinase at the nuclear periphery
    • Preller A, Wilson JE: Localization of the type III isozyme of hexokinase at the nuclear periphery. Arch Biochem Biophys 294: 482-492,1992
    • (1992) Arch Biochem Biophys , vol.294 , pp. 482-492
    • Preller, A.1    Wilson, J.E.2
  • 21
    • 0019162146 scopus 로고
    • Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing
    • Sanger F, Coulson AR, Barrel BG, Smith AJH, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol 143: 161-178, 1980
    • (1980) J Mol Biol , vol.143 , pp. 161-178
    • Sanger, F.1    Coulson, A.R.2    Barrel, B.G.3    Smith, A.J.H.4    Roe, B.A.5
  • 22
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS: Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67: 31-40, 1988
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 23
    • 0027234171 scopus 로고
    • Refolding an single-step purification of porcine interferon-γ from Escherichia coli inclusion bodies
    • Vandenbroeck K, Martens E, D'Andrea S, Billiau A: Refolding an single-step purification of porcine interferon-γ from Escherichia coli inclusion bodies. E J Biochem 215: 481-486, 1993
    • (1993) E J Biochem , vol.215 , pp. 481-486
    • Vandenbroeck, K.1    Martens, E.2    D'Andrea, S.3    Billiau, A.4
  • 25
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transfcrare (pGEX) fusion protein
    • Frangioni JV, Benjamin GN: Solubilization and purification of enzymatically active glutathione S-transfcrare (pGEX) fusion protein. Anal Biochem 210: 179-187, 1993
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Benjamin, G.N.2
  • 26
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE: Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem 192: 262-267, 1991
    • (1991) Anal Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2


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