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Volumn 9, Issue 6, 1999, Pages 861-869

Purification and characterization of Co2+-activated extracellular metalloprotease from Bacillus sp. JH108

Author keywords

Co2+ stimulated exopeptidase; Leucine aminopeptidase; Metalloprotease; Psychrotrophs

Indexed keywords

1,10 PHENANTHROLINE; AMMONIUM SULFATE; CYTOSOL AMINOPEPTIDASE; EDETIC ACID; METALLOPROTEINASE;

EID: 0033374747     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 0028406879 scopus 로고
    • Purification and characterization of an aminopeptidase from Lactobacillus casei subsp. rhamnosus S93
    • Arora, G. and B. H. Lee. 1994. Purification and characterization of an aminopeptidase from Lactobacillus casei subsp. rhamnosus S93. Biotechnol. Appl. Biochem. 19: 179-192.
    • (1994) Biotechnol. Appl. Biochem. , vol.19 , pp. 179-192
    • Arora, G.1    Lee, B.H.2
  • 2
    • 0027473733 scopus 로고
    • Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution
    • Ben-Meir, D., A. Spungin, R. Ashkenazi, and S. Blumberg. 1993. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur. J. Biochem. 212: 107-112.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 107-112
    • Ben-Meir, D.1    Spungin, A.2    Ashkenazi, R.3    Blumberg, S.4
  • 4
    • 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
  • 6
    • 0024643644 scopus 로고
    • Purification and properties of an aminopeptidase from Alaska pollack, Theragra chalcogramma, roe
    • Chiou, T. K., T. Matsui, and S. Konosu. 1989. Purification and properties of an aminopeptidase from Alaska pollack, Theragra chalcogramma, roe. J. Biochem. (Tokyo) 105: 505-509.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 505-509
    • Chiou, T.K.1    Matsui, T.2    Konosu, S.3
  • 7
    • 0025645610 scopus 로고
    • Purification and characterization of Acidolysin, an acidic metalloprotease produced by Clostridium acetobutylicum ATCC 824
    • Croux, C., V. Paquet, G. Goma, and P. Soucalille. 1990. Purification and characterization of Acidolysin, an acidic metalloprotease produced by Clostridium acetobutylicum ATCC 824. Appl. Environ. Microbiol. 56: 3634-3642.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3634-3642
    • Croux, C.1    Paquet, V.2    Goma, G.3    Soucalille, P.4
  • 8
    • 0022623552 scopus 로고
    • Isolation and characterization of a Vibrio aginolyticus mutant that overproduces extracellular proteases
    • Deane, S. M., F. T. Robb, and D. R Wood. 1986. Isolation and characterization of a Vibrio aginolyticus mutant that overproduces extracellular proteases. J. Gen. Microbiol. 132: 893-898.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 893-898
    • Deane, S.M.1    Robb, F.T.2    Wood, D.R.3
  • 11
    • 0024544124 scopus 로고
    • Strucutral gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase
    • Fukushima, J., S. Yamamoto, Y. Morihara, H. Atsumi, Takeuchi, S. Kawamoto, and K. Okuda. 1989. Strucutral gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase. J. Bacteriol. 171: 1698-1704.
    • (1989) J. Bacteriol. , vol.171 , pp. 1698-1704
    • Fukushima, J.1    Yamamoto, S.2    Morihara, Y.3    Atsumi, H.4    Takeuchi5    Kawamoto, S.6    Okuda, K.7
  • 12
    • 0016175428 scopus 로고
    • Human liver aminopeptidase. Role of metal ions in mechanism of action
    • Garner, C. W. and F. J. Behal. 1974. Human liver aminopeptidase. Role of metal ions in mechanism of action. Biochemistry 13: 3227-3233.
    • (1974) Biochemistry , vol.13 , pp. 3227-3233
    • Garner, C.W.1    Behal, F.J.2
  • 13
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidase: Properties and functions
    • Gonzales, T. and J. Robert-Baudroy. 1996. Bacterial aminopeptidase: Properties and functions. FEMS Microbiol. Rev. 18: 319-344.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudroy, J.2
  • 15
    • 0028118450 scopus 로고
    • Purification and characterization of an aminopeptidase from tuna Pyloric caeca
    • Hajjou, M. and Y. Le Gal. 1994. Purification and characterization of an aminopeptidase from tuna Pyloric caeca. Biochim. Biophys. Acta 1204: 1-13.
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 1-13
    • Hajjou, M.1    Le Gal, Y.2
  • 16
    • 0032427942 scopus 로고    scopus 로고
    • Characterization of alkaline serine proteases secreted from the coryneform bacterium TU-119
    • Kang, S. C., S. Park, and M. C. Choi. 1998. Characterization of alkaline serine proteases secreted from the coryneform bacterium TU-119. J. Microbiol. Biotechnol. 8: 639-644.
    • (1998) J. Microbiol. Biotechnol. , vol.8 , pp. 639-644
    • Kang, S.C.1    Park, S.2    Choi, M.C.3
  • 17
    • 1842301578 scopus 로고
    • Characteristics of Trypsin-like protease and metalloprotease associated with mycelium differentiation of Streptomyces albidoflavus SMF 301
    • Kang, S. G., B. C. Jeong, and K. J. Lee. 1995. Characteristics of Trypsin-like protease and metalloprotease associated with mycelium differentiation of Streptomyces albidoflavus SMF 301. J. Kor. Microbiol. 33: 304-314.
    • (1995) J. Kor. Microbiol. , vol.33 , pp. 304-314
    • Kang, S.G.1    Jeong, B.C.2    Lee, K.J.3
  • 18
    • 0020195866 scopus 로고
    • Purification and characterization of an aminopeptidase from porcine liver
    • Kawata, S., T. Imamura, K. Ninomiya, and S. Makisumi. 1982. Purification and characterization of an aminopeptidase from porcine liver. J. Biochem. 92: 1093-1101.
    • (1982) J. Biochem. , vol.92 , pp. 1093-1101
    • Kawata, S.1    Imamura, T.2    Ninomiya, K.3    Makisumi, S.4
  • 20
    • 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 277: 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0025806344 scopus 로고
    • Characterization of a metalloprotease from psychrophilic Xanthomonas maltophila
    • Margesin, R. and F. Schinner. 1991. Characterization of a metalloprotease from psychrophilic Xanthomonas maltophila. FEMS Microbiol. Lett. 79: 257-262.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 257-262
    • Margesin, R.1    Schinner, F.2
  • 22
    • 0018939483 scopus 로고
    • Purification and properties of human intestine alanine aminopeptidase
    • McClellan, J. B. and C. W. Garner. 1980. Purification and properties of human intestine alanine aminopeptidase. Biochim. Biophys. Acta 613: 160-167.
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 160-167
    • McClellan, J.B.1    Garner, C.W.2
  • 23
    • 0038418145 scopus 로고
    • Low-temperature environments
    • Academic Press, San Diego, U.S.A.
    • Morita, R. Y. 1992. Low-temperature environments. pp. 625-637. Encyclopedia of Microbiology, vol. 2, Academic Press, San Diego, U.S.A.
    • (1992) Encyclopedia of Microbiology , vol.2 , pp. 625-637
    • Morita, R.Y.1
  • 24
    • 0016381854 scopus 로고
    • Purification and properties of an extracelluar proteinase of psychrophilic Escherichia freundii
    • Nakazima, M., K. Mizusawa, and F. Yoshida. 1974. Purification and properties of an extracelluar proteinase of psychrophilic Escherichia freundii. Eur. J. Biochem. 44: 87-96.
    • (1974) Eur. J. Biochem. , vol.44 , pp. 87-96
    • Nakazima, M.1    Mizusawa, K.2    Yoshida, F.3
  • 25
    • 0026184666 scopus 로고
    • Purification and properties of aminopeptidase C from chicken skeletal muscle
    • Nishimura, T., Y. Kato, A. Okitani, and H. Kato. 1991, Purification and properties of aminopeptidase C from chicken skeletal muscle. Agr. Biol. Chem. 55: 1771-1778.
    • (1991) Agr. Biol. Chem. , vol.55 , pp. 1771-1778
    • Nishimura, T.1    Kato, Y.2    Okitani, A.3    Kato, H.4
  • 28
    • 0028119687 scopus 로고
    • Extracellular protease from Bacillus coagulans, a psychrotropic, antarctic bacterium - Production, purification and characterization
    • Sai Ram, M., L. Singh, S. I. Alam, and M. K. Aggarwal. 1994. Extracellular protease from Bacillus coagulans, a psychrotropic, antarctic bacterium - production, purification and characterization. J. Microbiol. Biotechnol. 10: 356-360.
    • (1994) J. Microbiol. Biotechnol. , vol.10 , pp. 356-360
    • Sai Ram, M.1    Singh, L.2    Alam, S.I.3    Aggarwal, M.K.4
  • 29
    • 0018875451 scopus 로고
    • Multiple molecular forms of human pancreas alanine aminopeptidase
    • Shidorowicz, W., G. C. Jackson, and F. J. Behal. 1980. Multiple molecular forms of human pancreas alanine aminopeptidase. Clin. Chim. Acta 104: 169-179.
    • (1980) Clin. Chim. Acta , vol.104 , pp. 169-179
    • Shidorowicz, W.1    Jackson, G.C.2    Behal, F.J.3
  • 31
    • 0001621050 scopus 로고
    • Bacillus stearothermophilus KP1236 neutral protease with strong thermostability comparable to thermolysin
    • Takii, Y., H. Taguchi, H. Shimoto, and Y. Suzuki. 1987. Bacillus stearothermophilus KP1236 neutral protease with strong thermostability comparable to thermolysin. Appl. Microbiol. Biotechnol. 27: 186-191.
    • (1987) Appl. Microbiol. Biotechnol. , vol.27 , pp. 186-191
    • Takii, Y.1    Taguchi, H.2    Shimoto, H.3    Suzuki, Y.4
  • 32
    • 0017230016 scopus 로고
    • The relative binding of cobalt and zinc to leucine aminopeptiase and the effect of cobalt substitution on specific activity
    • Thompson, G. A. and F. H. Carpenter. 1976. The relative binding of cobalt and zinc to leucine aminopeptiase and the effect of cobalt substitution on specific activity. J. Biol. Chem. 25: 1618-1624.
    • (1976) J. Biol. Chem. , vol.25 , pp. 1618-1624
    • Thompson, G.A.1    Carpenter, F.H.2
  • 33
    • 0025001523 scopus 로고
    • A chloride activated alanine aminopeptidase from melanoma cell line
    • Tsushima, H. and V. K. Hopsu-Havu. 1990. A chloride activated alanine aminopeptidase from melanoma cell line. Neoplasma 37: 415-425.
    • (1990) Neoplasma , vol.37 , pp. 415-425
    • Tsushima, H.1    Hopsu-Havu, V.K.2
  • 35
    • 0019890799 scopus 로고
    • Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney Leucine aminopeptidase
    • Van Wart, H. E. and S. H. Lin, 1981. Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney Leucine aminopeptidase. Biochemistry 20: 5682-5689.
    • (1981) Biochemistry , vol.20 , pp. 5682-5689
    • Van Wart, H.E.1    Lin, S.H.2
  • 36
    • 0030163049 scopus 로고    scopus 로고
    • An intracellular aminopeptidase from Streptomyces rimosus that prefers basic amino acids
    • Vitale, L., I. Skrtic, and M. Abramic. 1996. An intracellular aminopeptidase from Streptomyces rimosus that prefers basic amino acids. Arch. Microbiol. 165: 409-414.
    • (1996) Arch. Microbiol. , vol.165 , pp. 409-414
    • Vitale, L.1    Skrtic, I.2    Abramic, M.3
  • 37
    • 0019440573 scopus 로고
    • Purification and characterization of an enkephalin aminopeptidase from rat brain
    • Wagner, G. W., M. A. Tavianini, K. M. Harrmann, and J. E. Dixon. 1981. Purification and characterization of an enkephalin aminopeptidase from rat brain. Biochemistry 20: 3884-3890.
    • (1981) Biochemistry , vol.20 , pp. 3884-3890
    • Wagner, G.W.1    Tavianini, M.A.2    Harrmann, K.M.3    Dixon, J.E.4
  • 38
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinators by the dodecylsulfate-polyacrylamide gel electrophoresis
    • Weber, K. and M. Osborn. 1969. The reliability of molecular weight determinators by the dodecylsulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244: 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 39
    • 0032569016 scopus 로고    scopus 로고
    • Purification, characterization and cloning of a cytosolic Aspartyl aminopeptidase
    • Wilk, S., E. Wilk, and R. P. Magnusson. 1998. Purification, characterization and cloning of a cytosolic Aspartyl aminopeptidase. J. Biol. Chem. 273: 15961-15970.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15961-15970
    • Wilk, S.1    Wilk, E.2    Magnusson, R.P.3
  • 40
    • 0021228872 scopus 로고
    • Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro derived deletion mutation
    • Yang, M. Y., E. Ferrari, and D. J. Henner. 1984. Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro derived deletion mutation. J. Bacteriol. 160: 15-21.
    • (1984) J. Bacteriol. , vol.160 , pp. 15-21
    • Yang, M.Y.1    Ferrari, E.2    Henner, D.J.3
  • 41
    • 0022652268 scopus 로고
    • Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli
    • Yanagida, N., T. Uozumi, and T. Beppu. 1986. Specific excretion of Serratia marcescens protease through the outer membrane of Escherichia coli. J. Bacteriol. 166: 937-944.
    • (1986) J. Bacteriol. , vol.166 , pp. 937-944
    • Yanagida, N.1    Uozumi, T.2    Beppu, T.3


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