메뉴 건너뛰기




Volumn 181, Issue 3, 1999, Pages 833-840

Immunochemical analysis of UMP kinase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; EPITOPE; GUANOSINE TRIPHOSPHATE; MONOCLONAL ANTIBODY; NUCLEOSIDE MONOPHOSPHATE KINASE; POLYCLONAL ANTIBODY; UNCLASSIFIED DRUG; URIDINE PHOSPHATE KINASE; URIDINE TRIPHOSPHATE;

EID: 0032916705     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.3.833-840.1999     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0028998836 scopus 로고
    • 5A, showing the pathway of phosphoryl transfer
    • 5A, showing the pathway of phosphoryl transfer. Protein Sci. 4:1262-1271.
    • (1995) Protein Sci. , vol.4 , pp. 1262-1271
    • Abele, U.1    Schulz, G.E.2
  • 3
    • 0027448592 scopus 로고
    • Relation structure-fonction chez les enzymes ATP-dépendants, vue à travers la plus petite phosphotransférase, l'adényl kinase
    • Bârzu, O., and A.-M. Gilles. 1993. Relation structure-fonction chez les enzymes ATP-dépendants, vue à travers la plus petite phosphotransférase, l'adényl kinase. Ann. Inst. Pasteur/Actualités 4:121-132.
    • (1993) Ann. Inst. Pasteur/Actualités , vol.4 , pp. 121-132
    • Bârzu, O.1    Gilles, A.-M.2
  • 4
    • 0025348302 scopus 로고
    • Improved sectioning and ultrastructure of bacteria and animal cells embedded in Lowicryl
    • Benichou, J. C., C. Frehel, and A. Ryter. 1990. Improved sectioning and ultrastructure of bacteria and animal cells embedded in Lowicryl. J. Electron Microsc. Technique 14:289-297.
    • (1990) J. Electron Microsc. Technique , vol.14 , pp. 289-297
    • Benichou, J.C.1    Frehel, C.2    Ryter, A.3
  • 5
    • 0028291887 scopus 로고
    • Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system
    • Blondin, C., L. Serina, L. Wiesmüller, A.-M. Gilles, and O. Bârzu. 1994. Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system. Anal. Biochem. 220:219-221.
    • (1994) Anal. Biochem. , vol.220 , pp. 219-221
    • Blondin, C.1    Serina, L.2    Wiesmüller, L.3    Gilles, A.-M.4    Bârzu, O.5
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0031172544 scopus 로고    scopus 로고
    • Bovine serum albumin (BSA) as a reagent against non-specific immunogold labeling on LR-white and epoxy resin
    • Brorson, S. H. 1997. Bovine serum albumin (BSA) as a reagent against non-specific immunogold labeling on LR-White and epoxy resin. Micron 28:189-195.
    • (1997) Micron , vol.28 , pp. 189-195
    • Brorson, S.H.1
  • 9
    • 0023887425 scopus 로고
    • Refined structure porcine cytosolic adenylate kinase at 2.1 Å resolution
    • Dreusicke, D., P. A. Karplus, and G. E. Schulz. 1988. Refined structure porcine cytosolic adenylate kinase at 2.1 Å resolution. J. Mol. Biol. 199:359-371.
    • (1988) J. Mol. Biol. , vol.199 , pp. 359-371
    • Dreusicke, D.1    Karplus, P.A.2    Schulz, G.E.3
  • 10
    • 0028945093 scopus 로고
    • The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli
    • Fricke, J., J. Neuhard, R. A. Kelln, and S. Pedersen. 1995. The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli. J. Bacteriol. 177:517-523.
    • (1995) J. Bacteriol. , vol.177 , pp. 517-523
    • Fricke, J.1    Neuhard, J.2    Kelln, R.A.3    Pedersen, S.4
  • 11
    • 0021964141 scopus 로고
    • Measurements of the true-affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., A. F. Charlotte, L. Djavadi-Ohaniance, and M. E. Goldberg. 1985. Measurements of the true-affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77:305-319
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Charlotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 12
    • 0020971322 scopus 로고
    • Quantitative two-dimensional electrophoresis of proteins
    • Garrels, J. I. 1983. Quantitative two-dimensional electrophoresis of proteins. Methods Enzymol. 100:411-423.
    • (1983) Methods Enzymol. , vol.100 , pp. 411-423
    • Garrels, J.I.1
  • 13
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase joints on either side of two helices close like neighboring lingers
    • Gerstein, M., G. Schulz, and C. Chothia. 1993. Domain closure in adenylate kinase joints on either side of two helices close like neighboring lingers. J. Mol. Biol. 229:494-501.
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.2    Chothia, C.3
  • 14
    • 0020079808 scopus 로고
    • Adenylate kinase of Escherichia coli: Evidence for a functional interaction in phospholipid synthesis
    • Goelz, S. E., and J. E. Cronan, Jr. 1982. Adenylate kinase of Escherichia coli: evidence for a functional interaction in phospholipid synthesis. Biochemistry 21:189-195.
    • (1982) Biochemistry , vol.21 , pp. 189-195
    • Goelz, S.E.1    Cronan J.E., Jr.2
  • 15
    • 0032145388 scopus 로고    scopus 로고
    • Modification of unicryl composition for rapid polymerization at low temperature without alteration of immunocytochemical sensitivity
    • Gounon, P., and J.-P. Rolland. 1998. Modification of unicryl composition for rapid polymerization at low temperature without alteration of immunocytochemical sensitivity. Micron 29:293-296.
    • (1998) Micron , vol.29 , pp. 293-296
    • Gounon, P.1    Rolland, J.-P.2
  • 16
    • 0032563126 scopus 로고    scopus 로고
    • pyrH-encoded UMP-kinase directly participates in pyrimidine-specific modulation of promoter activity in Escherichia coli
    • Kholti, A., D. Charlier, D. Gigot, N. Huysveld, M. Roovers, and N. Glansdorff. 1998. pyrH-encoded UMP-kinase directly participates in pyrimidine-specific modulation of promoter activity in Escherichia coli. J. Mol. Biol. 280:571-582.
    • (1998) J. Mol. Biol. , vol.280 , pp. 571-582
    • Kholti, A.1    Charlier, D.2    Gigot, D.3    Huysveld, N.4    Roovers, M.5    Glansdorff, N.6
  • 17
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G., and C. Milstein. 1975. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0344525935 scopus 로고    scopus 로고
    • Unpublished data
    • 18a. Landais, S., et al. Unpublished data.
    • Landais, S.1
  • 20
    • 0030983671 scopus 로고    scopus 로고
    • Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response. Identification of targets by two-dimensional electrophoresis
    • Laurent-Winter, C., S. Ngo, A. Danchin, and P. Bertin. 1997. Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response. Identification of targets by two-dimensional electrophoresis. Eur. J. Biochem. 244:767-773.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 767-773
    • Laurent-Winter, C.1    Ngo, S.2    Danchin, A.3    Bertin, P.4
  • 21
    • 0029941281 scopus 로고    scopus 로고
    • Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism
    • Lu, Q., and M. Inouye. 1996. Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism. Proc. Natl. Acad. Sci. USA 93:5720-5725.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5720-5725
    • Lu, Q.1    Inouye, M.2
  • 22
    • 0001420820 scopus 로고
    • A modified procedure for leading staining of thin sections
    • Millonig, G. 1961. A modified procedure for leading staining of thin sections. J. Biophys. Biochem. Cytol. 11:736-739.
    • (1961) J. Biophys. Biochem. Cytol. , vol.11 , pp. 736-739
    • Millonig, G.1
  • 23
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey, J. H. 1981. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117:307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 24
    • 0026544877 scopus 로고
    • 5A refined at 1.9 Å resolution. A model for a catalytic transition state
    • 5A refined at 1.9 Å resolution. A model for a catalytic transition state. J. Mol. Biol. 224:159-177.
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Müller, C.W.1    Schulz, G.E.2
  • 25
    • 0028327709 scopus 로고
    • The structure of uridylate kinase with its substrates, showing the transition state geometry
    • Müller-Dieckmann, H.-J., and G. E. Schultz. 1994. The structure of uridylate kinase with its substrates, showing the transition state geometry. J. Mol. Biol. 236:361-367.
    • (1994) J. Mol. Biol. , vol.236 , pp. 361-367
    • Müller-Dieckmann, H.-J.1    Schultz, G.E.2
  • 26
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulinbinding domains of Bordetella pertussis adenylate cyclase
    • Munier, H., A.-M. Gilles, P. Glaser, E. Krin, A. Danchin, R. S. Sarfati, and O. Bârzu. 1991. Isolation and characterization of catalytic and calmodulinbinding domains of Bordetella pertussis adenylate cyclase. Eur. J. Biochem. 196:469-474.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.-M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.S.6    Bârzu, O.7
  • 28
    • 0030002871 scopus 로고    scopus 로고
    • Escherichia coli thymidilate kinase: Molecular cloning, nucleotide sequence, and genetic organization of the corresponding tmk locus
    • Reynes, J.-P., M. Tiraby, M. Baron, D. Drocourt, and G. Tiraby. 1996. Escherichia coli thymidilate kinase: molecular cloning, nucleotide sequence, and genetic organization of the corresponding tmk locus. J. Bacteriol. 178:2804-2812.
    • (1996) J. Bacteriol. , vol.178 , pp. 2804-2812
    • Reynes, J.-P.1    Tiraby, M.2    Baron, M.3    Drocourt, D.4    Tiraby, G.5
  • 32
    • 0028953772 scopus 로고
    • Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP
    • Serina, L., C. Blondin, E. Krin, O. Sismeiro, A. Danchin, H. Sakamoto, A.-M. Gilles, and O. Bârzu. 1995. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34:5066-5074.
    • (1995) Biochemistry , vol.34 , pp. 5066-5074
    • Serina, L.1    Blondin, C.2    Krin, E.3    Sismeiro, O.4    Danchin, A.5    Sakamoto, H.6    Gilles, A.-M.7    Bârzu, O.8
  • 34
    • 0011106749 scopus 로고
    • Cloning, nucleotide sequence and expression of the Escherichia coli K-12 pyrH gene encoding UMP kinase
    • Smallshaw, J., and R. A. Kelln. 1992. Cloning, nucleotide sequence and expression of the Escherichia coli K-12 pyrH gene encoding UMP kinase. Genetics (Life Sci. Adv.) 11:59-65.
    • (1992) Genetics (Life Sci. Adv.) , vol.11 , pp. 59-65
    • Smallshaw, J.1    Kelln, R.A.2
  • 35
    • 0344525925 scopus 로고    scopus 로고
    • Unpublished data
    • 33a. Sourdive, D. Unpublished data.
    • Sourdive, D.1
  • 37
    • 0025887633 scopus 로고
    • Mechanism of adenylate kinase: Site-directed mutagenesis versus X-ray and NMR
    • Tsai, M.-D., and H. Yan. 1991. Mechanism of adenylate kinase: site-directed mutagenesis versus X-ray and NMR. Biochemistry 30:6806-6818.
    • (1991) Biochemistry , vol.30 , pp. 6806-6818
    • Tsai, M.-D.1    Yan, H.2
  • 38
    • 0000087068 scopus 로고    scopus 로고
    • Gene-protein database of Escherichia coli K-12
    • edition 6, F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). American Society for Microbiology, Washington, D.C.
    • VanBogelen, R. A., K. Z. Abshire, A. Pertsemlidis, R. L. Clark, and F. C. Neidhardt. 1996. Gene-protein database of Escherichia coli K-12, edition 6, p. 2067-2117. In F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molec ular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molec Ular Biology, 2nd Ed. , pp. 2067-2117
    • VanBogelen, R.A.1    Abshire, K.Z.2    Pertsemlidis, A.3    Clark, R.L.4    Neidhardt, F.C.5
  • 39
    • 0016324662 scopus 로고
    • A microplate method of enzyme-linked immunosorbent assay and its application to malaria
    • Voller, A., D. Bidwell, G. Huldt, and E. Engvall. 1974. A microplate method of enzyme-linked immunosorbent assay and its application to malaria. Bull. W. H. O. 51:209-211.
    • (1974) Bull. W. H. O. , vol.51 , pp. 209-211
    • Voller, A.1    Bidwell, D.2    Huldt, G.3    Engvall, E.4
  • 40
    • 0026485123 scopus 로고
    • Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli
    • Yamanaka, K., T. Ogura, H. Niki, and S. Hiraga. 1992. Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli. J. Bacteriol. 174:7517-7526.
    • (1992) J. Bacteriol. , vol.174 , pp. 7517-7526
    • Yamanaka, K.1    Ogura, T.2    Niki, H.3    Hiraga, S.4
  • 41
    • 0028220659 scopus 로고
    • Multi-copy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli
    • Yamanaka, K., T. Ogura, E. V. Koonin, H. Niki, and S. Hiraga. 1994. Multi-copy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli. Mol. Gen. Genet. 243:9-16.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 9-16
    • Yamanaka, K.1    Ogura, T.2    Koonin, E.V.3    Niki, H.4    Hiraga, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.