메뉴 건너뛰기




Volumn 63, Issue 2, 1997, Pages 408-413

Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CHITIN; CHITINASE; DNA;

EID: 0030981929     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.2.408-413.1997     Document Type: Article
Times cited : (118)

References (24)
  • 1
    • 0026315624 scopus 로고
    • Chitin utilization by marine bacteria: Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii
    • Bassler, B. L., C. Yu, Y. C. Lee, and S. Roseman. 1991. Chitin utilization by marine bacteria: degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266:24276-24286.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24276-24286
    • Bassler, B.L.1    Yu, C.2    Lee, Y.C.3    Roseman, S.4
  • 3
    • 0003133857 scopus 로고
    • The ecology of chitin degradation
    • Gooday, G. W. 1990. The ecology of chitin degradation. Adv. Microb. Ecol. 11:387-430.
    • (1990) Adv. Microb. Ecol. , vol.11 , pp. 387-430
    • Gooday, G.W.1
  • 5
    • 0024316572 scopus 로고
    • Nucleotide sequence of the chitinase B gene of Serratia marcescens
    • Harpster, M. H., and P. Dunsmuir. 1989. Nucleotide sequence of the chitinase B gene of Serratia marcescens. Nucleic Acids Res. 17:5395.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5395
    • Harpster, M.H.1    Dunsmuir, P.2
  • 6
    • 0029690139 scopus 로고    scopus 로고
    • Anomalous estimation of protease molecular weights using gelatin-containing SDS-PAGE
    • Hummel, K. M., A. R. Penheiter, A. C. Gathman, and W. W. Lilly. 1996. Anomalous estimation of protease molecular weights using gelatin-containing SDS-PAGE. Anal. Biochem. 233:140-142.
    • (1996) Anal. Biochem. , vol.233 , pp. 140-142
    • Hummel, K.M.1    Penheiter, A.R.2    Gathman, A.C.3    Lilly, W.W.4
  • 7
    • 0023387947 scopus 로고
    • Translocation of Vibrio harveyi N,N′-diacetylchitobiase to the outer membrane of Escherichia coli
    • Jannatipour, M., R. W. Soto-Gil, L. C. Childers, and J. W. Zyskind. 1987. Translocation of Vibrio harveyi N,N′-diacetylchitobiase to the outer membrane of Escherichia coli. J. Bacteriol. 169:3785-3791.
    • (1987) J. Bacteriol. , vol.169 , pp. 3785-3791
    • Jannatipour, M.1    Soto-Gil, R.W.2    Childers, L.C.3    Zyskind, J.W.4
  • 8
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones, J. D. G., K. L. Grady, T. V. Suslow, and J. R. Bedbrook. 1986. Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J. 5:467-173.
    • (1986) EMBO J. , vol.5 , pp. 467-1173
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 9
    • 0025834867 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66
    • Miyashita, K., T. Fujii, and Y. Sawada. 1991. Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66. J. Gen. Microbiol. 137:2065-2072.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2065-2072
    • Miyashita, K.1    Fujii, T.2    Sawada, Y.3
  • 10
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano, J., A. Durán, and E. Cabib. 1977. A rapid and sensitive assay for chitinase using tritiated chitin. Anal. Biochem. 83:648-656.
    • (1977) Anal. Biochem. , vol.83 , pp. 648-656
    • Molano, J.1    Durán, A.2    Cabib, E.3
  • 11
    • 0027474233 scopus 로고
    • Role of chitin-binding proteins in the specific attachment of the marine bacterium Vibrio harveyi to chitin
    • Montgomery, M. T., and D. L. Kirchman. 1993. Role of chitin-binding proteins in the specific attachment of the marine bacterium Vibrio harveyi to chitin. Appl. Environ. Microbiol. 59:373-379.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 373-379
    • Montgomery, M.T.1    Kirchman, D.L.2
  • 12
    • 0028153318 scopus 로고
    • Induction of chitin-binding proteins during the specific attachment of the marine bacterium Vibrio harveyi to chitin
    • Montgomery, M. T., and D. L. Kirchman, 1994. Induction of chitin-binding proteins during the specific attachment of the marine bacterium Vibrio harveyi to chitin. Appl. Environ. Microbiol. 60:4284-4288.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4284-4288
    • Montgomery, M.T.1    Kirchman, D.L.2
  • 13
    • 0004184147 scopus 로고
    • Pergamon Press, Oxford, United Kingdom
    • Muzzarelli, R. A. A. 1977. Chitin, p. 155-181. Pergamon Press, Oxford, United Kingdom.
    • (1977) Chitin , pp. 155-181
    • Muzzarelli, R.A.A.1
  • 14
    • 0028308476 scopus 로고
    • The 92 kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus
    • Radwin, H. H., H. J. Plattner, U. Menge, and H. Diekmann. 1994. The 92 kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus. FEMS Microbiol. Lett. 120:31-36.
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 31-36
    • Radwin, H.H.1    Plattner, H.J.2    Menge, U.3    Diekmann, H.4
  • 15
    • 0020392369 scopus 로고
    • Serratia marcescens chitinase: One-step purification and use for the determination of chitin
    • Roberts, R. L., and E. Cabib. 1982. Serratia marcescens chitinase: one-step purification and use for the determination of chitin. Anal. Biochem. 127: 402-412.
    • (1982) Anal. Biochem. , vol.127 , pp. 402-412
    • Roberts, R.L.1    Cabib, E.2
  • 16
    • 0028163799 scopus 로고
    • A radiochemical method for secondary production in planktonic crustacea based on rate of chitin synthesis
    • Roff, J. C., J. T. Kroetsch, and A. J. Clarke. 1994. A radiochemical method for secondary production in planktonic crustacea based on rate of chitin synthesis. J. Plankton Res. 16:961-976.
    • (1994) J. Plankton Res. , vol.16 , pp. 961-976
    • Roff, J.C.1    Kroetsch, J.T.2    Clarke, A.J.3
  • 17
    • 0026772129 scopus 로고
    • Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity
    • Romaguera, A., U. Menge, R. Breves, and H. Diekmann. 1992. Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity. J. Bacteriol. 174:3450-3454.
    • (1992) J. Bacteriol. , vol.174 , pp. 3450-3454
    • Romaguera, A.1    Menge, U.2    Breves, R.3    Diekmann, H.4
  • 18
    • 0028070108 scopus 로고
    • The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms
    • Schnellmann, J., A. Zeltins, H. Blaak, and H. Schrempf. 1994. The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms. Mol. Microbiol. 13:807-819.
    • (1994) Mol. Microbiol. , vol.13 , pp. 807-819
    • Schnellmann, J.1    Zeltins, A.2    Blaak, H.3    Schrempf, H.4
  • 19
    • 0026070379 scopus 로고
    • Rapid mapping by transposon mulagenesis of epitopes on the muscular dystrophy protein, dystrophin
    • Sedgwick, S. C., T. M. Nguyen, J. M. Ellis, H. Crowne, and G. E. Morris. 1991. Rapid mapping by transposon mulagenesis of epitopes on the muscular dystrophy protein, dystrophin. Nucleic Acids Res. 19:5889-5894.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5889-5894
    • Sedgwick, S.C.1    Nguyen, T.M.2    Ellis, J.M.3    Crowne, H.4    Morris, G.E.5
  • 20
    • 0028107180 scopus 로고
    • Enzymatic degradation of chitins and partially deacetylated chitins
    • Shigemasa, Y., K. Saito, H. Sashiwa, and H. Saimoto. 1994. Enzymatic degradation of chitins and partially deacetylated chitins. Int. J. Biol. Macromol. 16:43-49.
    • (1994) Int. J. Biol. Macromol. , vol.16 , pp. 43-49
    • Shigemasa, Y.1    Saito, K.2    Sashiwa, H.3    Saimoto, H.4
  • 21
    • 0343567800 scopus 로고
    • Ph.D. dissertation. University of California, San Diego, and San Diego State University, San Diego, Calif.
    • Soto-Gil, R. W. 1988. Chitobiase and chitinase from Vibrio harveyi. Ph.D. dissertation. University of California, San Diego, and San Diego State University, San Diego, Calif.
    • (1988) Chitobiase and Chitinase from Vibrio Harveyi
    • Soto-Gil, R.W.1
  • 22
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel, J., and A. Asselin. 1989. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178:362-366.
    • (1989) Anal. Biochem. , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 23
    • 0027534187 scopus 로고
    • Cloning, sequence, and expression of a chitinase gene from a marine bacterium. Alteromonas sp. strain O-7
    • Tsujibo, H., H. Orikoshi, H. Tanno, K. Fujimoto, K. Miyamoto, L. Imada, Y. Okami, and Y. Inamori. 1993. Cloning, sequence, and expression of a chitinase gene from a marine bacterium. Alteromonas sp. strain O-7. J. Bacteriol. 175:176-181.
    • (1993) J. Bacteriol. , vol.175 , pp. 176-181
    • Tsujibo, H.1    Orikoshi, H.2    Tanno, H.3    Fujimoto, K.4    Miyamoto, K.5    Imada, L.6    Okami, Y.7    Inamori, Y.8
  • 24
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe, T., W. Oyanagi, K. Suzuki, and H. Tanaka. 1990. Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol. 172:4017-4022.
    • (1990) J. Bacteriol. , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.