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Volumn 6, Issue 2, 1999, Pages 137-152

Thermal stability of the cellulose synthase complex of Acetobacter xylinum

Author keywords

Acetobacter xylinum; Cellulose synthase; Thermostability

Indexed keywords

ANALYSIS; CELLULOSE; THERMAL PROPERTY;

EID: 0032835984     PISSN: 09690239     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1009208610922     Document Type: Article
Times cited : (5)

References (28)
  • 1
    • 0021892611 scopus 로고
    • The mechanism of irreversible enzyme inactivation at 100°C
    • Ahern, T. J. and Klibanov, A. M. (1985) The mechanism of irreversible enzyme inactivation at 100°C. Science 228, 1280-1284.
    • (1985) Science , vol.228 , pp. 1280-1284
    • Ahern, T.J.1    Klibanov, A.M.2
  • 2
    • 0026692622 scopus 로고
    • Stability of fungal α-amylase in sodium dodecyl sulfate
    • Arakawa, T., Hung, L. and Narhi, L. O. (1992) Stability of fungal α-amylase in sodium dodecyl sulfate. J. Prot. Chem. 11, 111-117.
    • (1992) J. Prot. Chem. , vol.11 , pp. 111-117
    • Arakawa, T.1    Hung, L.2    Narhi, L.O.3
  • 5
    • 0003303413 scopus 로고
    • In vitro synthesis of cellulose II from a cytoplasmic membrane fraction of Acetobacter xylinum
    • Bureau, T. E. and Brown, R. M., Jr. (1987) In vitro synthesis of cellulose II from a cytoplasmic membrane fraction of Acetobacter xylinum. Proc. Natl. Acad. Sci. 84, 6985-6989.
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 6985-6989
    • Bureau, T.E.1    Brown R.M., Jr.2
  • 6
    • 0001930816 scopus 로고    scopus 로고
    • Immunochemical studies of the cellulose synthase complex in Acetobacter xylinum
    • Chen, H. P. and Brown, R. M., Jr. (1996) Immunochemical studies of the cellulose synthase complex in Acetobacter xylinum. Cellulose 3: 63-75.
    • (1996) Cellulose , vol.3 , pp. 63-75
    • Chen, H.P.1    Brown R.M., Jr.2
  • 7
    • 0026713762 scopus 로고
    • Identification of hydrophobic proteins FepD and FepG of the Escherichia coli ferrienterobactin permease
    • Chenault, S. S. and Earhart, C. F. (1992) Identification of hydrophobic proteins FepD and FepG of the Escherichia coli ferrienterobactin permease. J. Gen. Microbiol. 138, 2167-2171.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2167-2171
    • Chenault, S.S.1    Earhart, C.F.2
  • 8
    • 0026406989 scopus 로고
    • Functionally-stabilized proteins-a review
    • Fágáin, C. Ó. and O'Kennedy, R. (1991) Functionally-stabilized proteins-a review. Biotech. Adv. 9, 351-409.
    • (1991) Biotech. Adv. , vol.9 , pp. 351-409
    • Fágáin, C.Ó.1    O'Kennedy, R.2
  • 9
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides
    • Geiger, T. and Clarke, S. (1987) Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. J. Biol. Chem. 262, 785-794.
    • (1987) J. Biol. Chem. , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 10
    • 0028195932 scopus 로고
    • Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins
    • Gimel, J. C., Durand, D. and Nicolai, T. (1994) Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromol. 27, 583-589.
    • (1994) Macromol. , vol.27 , pp. 583-589
    • Gimel, J.C.1    Durand, D.2    Nicolai, T.3
  • 11
    • 0021728707 scopus 로고
    • Identification of the secY (prlA) gene product involved in protein export in Escherichia coli
    • Ito, K. (1984) Identification of the secY (prlA) gene product involved in protein export in Escherichia coli. Mol. Gen. Genetics 197, 204-208.
    • (1984) Mol. Gen. Genetics , vol.197 , pp. 204-208
    • Ito, K.1
  • 12
    • 0022998008 scopus 로고
    • Iron hydroxamate transport of Escherichia coli: Nucleotide sequence of the fluB gene and identification of the protein
    • Köster W. and Braun, V. (1986) Iron hydroxamate transport of Escherichia coli: Nucleotide sequence of the fluB gene and identification of the protein. Mol. Gen. Genetics 204, 435-442.
    • (1986) Mol. Gen. Genetics , vol.204 , pp. 435-442
    • Köster, W.1    Braun, V.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, E. 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, E.K.1
  • 14
    • 0003364682 scopus 로고
    • Purification of cellulose synthase from Acetobacter xylinum
    • C. Schuerch, ed., Wiley, New York
    • Lin, F. C. and Brown, R. M., Jr. (1989) Purification of cellulose synthase from Acetobacter xylinum. In: Cellulose and Wood-Chemistry and Technology (C. Schuerch, ed.), Wiley, New York, pp. 473-492.
    • (1989) Cellulose and Wood-Chemistry and Technology , pp. 473-492
    • Lin, F.C.1    Brown R.M., Jr.2
  • 16
    • 0000923841 scopus 로고
    • Gel electrophoresis of viral proteins
    • K. Maramorosch and H. Koprowski, eds, Academic Press, New York
    • Maizel, J. V., Jr. (1971) Gel electrophoresis of viral proteins. In: Methods of Virology (K. Maramorosch and H. Koprowski, eds), Vol. 5, Academic Press, New York, pp. 179-246.
    • (1971) Methods of Virology , vol.5 , pp. 179-246
    • Maizel J.V., Jr.1
  • 17
    • 0026077656 scopus 로고
    • Polypeptide composition of bacterial cyclic diguanylic acid dependent cellulose synthase and the occurrence of immunologically crossreacting proteins in higher plants
    • Mayer, R., Ross, P., Weinhouse, H., Amikam, D., Volman, G., Ohana, P., Calhoon, R. D., Wong, H. G., Emerick, A. W. and Benziman, M. (1991) Polypeptide composition of bacterial cyclic diguanylic acid dependent cellulose synthase and the occurrence of immunologically crossreacting proteins in higher plants. Proc. Natl. Acad. Sci. 88, 5472-5476.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 5472-5476
    • Mayer, R.1    Ross, P.2    Weinhouse, H.3    Amikam, D.4    Volman, G.5    Ohana, P.6    Calhoon, R.D.7    Wong, H.G.8    Emerick, A.W.9    Benziman, M.10
  • 18
    • 0020180323 scopus 로고
    • Inactivation and reactivation of proteins
    • Mozhaev, V. V. and Martinek, K. (1982) Inactivation and reactivation of proteins. Enz. Microb. Technol. 4, 299-309.
    • (1982) Enz. Microb. Technol. , vol.4 , pp. 299-309
    • Mozhaev, V.V.1    Martinek, K.2
  • 19
    • 0025022699 scopus 로고
    • Protein engineering for thermostability
    • Nosoh, Y. and Sekiguchi, T. (1990) Protein engineering for thermostability. Trends Biotech. 8, 16-20.
    • (1990) Trends Biotech. , vol.8 , pp. 16-20
    • Nosoh, Y.1    Sekiguchi, T.2
  • 20
    • 0026093011 scopus 로고
    • Cellulose biosynthesis and function in bacteria
    • Ross, P., Mayer, R. and Benziman, M. (1991) Cellulose biosynthesis and function in bacteria. Microbiol. Rev. 55, 35-58.
    • (1991) Microbiol. Rev. , vol.55 , pp. 35-58
    • Ross, P.1    Mayer, R.2    Benziman, M.3
  • 21
    • 0025521805 scopus 로고
    • Cloning and sequencing of the cellulose synthase catalytic subunit gene of A. xylinum
    • Saxena, I. M., Lin, F. C. and Brown, R. M., Jr. (1990) Cloning and sequencing of the cellulose synthase catalytic subunit gene of A. xylinum. Plant Mol. Biol. 15, 673-683.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 673-683
    • Saxena, I.M.1    Lin, F.C.2    Brown R.M., Jr.3
  • 22
    • 0026178016 scopus 로고
    • Identification of a new gene in an operon fro cellulose biosynthesis in Acetobacter xylinum
    • Saxena, I. M., Lin, F. C. and Brown, R. M., Jr. (1991) Identification of a new gene in an operon fro cellulose biosynthesis in Acetobacter xylinum. Plant Mol. Biol. 16, 947-954.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 947-954
    • Saxena, I.M.1    Lin, F.C.2    Brown R.M., Jr.3
  • 23
    • 0027959269 scopus 로고
    • Characterization of genes in the cellulose-synthesizing operon (acs operon) of Acetobacter xylinum: Implications for cellulose crystallization
    • Saxena, I. M., Kudlicka, K., Okuda, K. and Brown, R. M., Jr. (1994) Characterization of genes in the cellulose-synthesizing operon (acs operon) of Acetobacter xylinum: Implications for cellulose crystallization. J. Bacteriol. 176, 5735-5752.
    • (1994) J. Bacteriol. , vol.176 , pp. 5735-5752
    • Saxena, I.M.1    Kudlicka, K.2    Okuda, K.3    Brown R.M., Jr.4
  • 24
    • 0026950528 scopus 로고
    • An assessment of proteolytic enzyme in Tetrahymena thermophila
    • Straus, J. W., Migaki, G. and Finch, M. T. (1992) An assessment of proteolytic enzyme in Tetrahymena thermophila. J. Protozool. 39, 655-662.
    • (1992) J. Protozool. , vol.39 , pp. 655-662
    • Straus, J.W.1    Migaki, G.2    Finch, M.T.3
  • 25
    • 0022017344 scopus 로고
    • Stability of enzymes
    • Tombes, M. P. (1985) Stability of enzymes. J. Appl. Biochem. 7, 3-24.
    • (1985) J. Appl. Biochem. , vol.7 , pp. 3-24
    • Tombes, M.P.1
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0015437962 scopus 로고
    • Measurement of the molecular weight by electrophoresis on SDS-acrylamide gel
    • C. H. W. Hirs and S. N. Timasheff, eds, Academic Press, New York
    • Weber, K., Pringle, J. R. and Osborn, M. (1972) Measurement of the molecular weight by electrophoresis on SDS-acrylamide gel. In: Methods in Enzymology (C. H. W. Hirs and S. N. Timasheff, eds), Vol. 26, Academic Press, New York, pp. 3-27.
    • (1972) Methods in Enzymology , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3
  • 28
    • 0023055754 scopus 로고
    • Why does ribonuclease irreversibly inactivate at high temperatures?
    • Zale, S. E. and Klibanov, A. M. (1986) Why does ribonuclease irreversibly inactivate at high temperatures? Biochem. 25, 5432-5444.
    • (1986) Biochem. , vol.25 , pp. 5432-5444
    • Zale, S.E.1    Klibanov, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.