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Volumn 70, Issue 6, 2004, Pages 3321-3328

Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; DATABASE SYSTEMS; ENZYMES; HYDROPHOBICITY; POLYMERS; PURIFICATION;

EID: 2942560270     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.6.3321-3328.2004     Document Type: Article
Times cited : (147)

References (60)
  • 2
    • 0002188092 scopus 로고
    • Microbial life at low temperatures: Ecological aspects
    • D. J. Kushner (ed.). Academic Press, New York, N.Y.
    • Baross, J. A., and R. Y. Morita. 1978. Microbial life at low temperatures: ecological aspects, p. 7-91. In D. J. Kushner (ed.), Microbial life in extreme environments. Academic Press, New York, N.Y.
    • (1978) Microbial Life in Extreme Environments , pp. 7-91
    • Baross, J.A.1    Morita, R.Y.2
  • 3
    • 0034788845 scopus 로고    scopus 로고
    • New method for exopolysaccharide determination in culture broth using stirred ultrafiltration cells
    • Bergmaier, D., C. Lacroix, M. G. Macedo, and C. P. Champagne. 2001. New method for exopolysaccharide determination in culture broth using stirred ultrafiltration cells. Appl. Microbiol. Biotechnol. 57:401-406.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 401-406
    • Bergmaier, D.1    Lacroix, C.2    Macedo, M.G.3    Champagne, C.P.4
  • 4
    • 0029103125 scopus 로고
    • Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase
    • Blomster, M., A. Wetterholm, M. J. Mueller, and J. Z. Haeggstrom. 1995. Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase. Eur. J. Biochem. 231:528-534.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 528-534
    • Blomster, M.1    Wetterholm, A.2    Mueller, M.J.3    Haeggstrom, J.Z.4
  • 5
    • 0028014604 scopus 로고
    • On the relevance of sequence statistics for the properties of extremophilic proteins
    • Bohm, G., and R. Jaenicke. 1994. On the relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Pept. Protein Res. 43:97-106.
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 97-106
    • Bohm, G.1    Jaenicke, R.2
  • 6
    • 2942575397 scopus 로고    scopus 로고
    • Isolation and characterization of marine psychrophilic phage-host systems from Arctic sea ice
    • Borriss, M., E. Helmke, R. Hanschke, and T. Schweder. 2003. Isolation and characterization of marine psychrophilic phage-host systems from Arctic sea ice. Extremophiles 7:377-384.
    • (2003) Extremophiles , vol.7 , pp. 377-384
    • Borriss, M.1    Helmke, E.2    Hanschke, R.3    Schweder, T.4
  • 7
    • 0031753313 scopus 로고    scopus 로고
    • Colwellia demingiae sp. nov., Colwellia homerae sp. nov., Colwellia rossensis sp. nov., and Colwellia psychrotropica sp. nov.: Psychrophilic Antarctic species with the ability to synthesize docosahexaenoic acid (22:5ω3)
    • Bowman, J. P., J. J. Gosink, S. A. McCammon, T. E. Lewis, D. S. Nichols, P. D. Nichols, J. H. Skerratt, J. T. Staley, and T. A. McMeekin. 1998. Colwellia demingiae sp. nov., Colwellia homerae sp. nov., Colwellia rossensis sp. nov., and Colwellia psychrotropica sp. nov.: psychrophilic Antarctic species with the ability to synthesize docosahexaenoic acid (22:5ω3). Int. J. Syst. Bacteriol. 48:1171-1180.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1171-1180
    • Bowman, J.P.1    Gosink, J.J.2    McCammon, S.A.3    Lewis, T.E.4    Nichols, D.S.5    Nichols, P.D.6    Skerratt, J.H.7    Staley, J.T.8    McMeekin, T.A.9
  • 8
    • 2942543766 scopus 로고    scopus 로고
    • Distribution, ecology and taxonomy of psychrophilic bacteria
    • in press
    • Bowman, J. P. Distribution, ecology and taxonomy of psychrophilic bacteria. Adv. Microb. Ecol., in press.
    • Adv. Microb. Ecol.
    • Bowman, J.P.1
  • 9
    • 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
  • 10
    • 0030513148 scopus 로고    scopus 로고
    • Psychrophilic microorganisms and their cold-active enzymes
    • Brenchley, J. E. 1996. Psychrophilic microorganisms and their cold-active enzymes. J. Ind. Microbiol. 17:432-437.
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 432-437
    • Brenchley, J.E.1
  • 11
    • 0034660603 scopus 로고    scopus 로고
    • Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species
    • Chessa, J.-P., I. Petrescu, M. Bentahir, J. V. Beeumen, and C. Gerday. 2000. Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species. Biochim. Biophys. Acta 1479:265-274.
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 265-274
    • Chessa, J.-P.1    Petrescu, I.2    Bentahir, M.3    Beeumen, J.V.4    Gerday, C.5
  • 12
    • 0032484910 scopus 로고    scopus 로고
    • Spontaneous assembly of marine dissolved organic matter into polymer gels
    • Chin, W.-C., M. V. Orellana, and P. Verdugo. 1998. Spontaneous assembly of marine dissolved organic matter into polymer gels. Nature 391:568-571.
    • (1998) Nature , vol.391 , pp. 568-571
    • Chin, W.-C.1    Orellana, M.V.2    Verdugo, P.3
  • 13
    • 0028929584 scopus 로고
    • Sequence analysis, distribution and expression of an aminopeptidase N-encoding gene from Lactobacillus helveticus CNRZ32
    • Christensen, J. E., D. L. Lin, A. Palva, and J. L. Steele. 1995. Sequence analysis, distribution and expression of an aminopeptidase N-encoding gene from Lactobacillus helveticus CNRZ32. Gene 155:89-93.
    • (1995) Gene , vol.155 , pp. 89-93
    • Christensen, J.E.1    Lin, D.L.2    Palva, A.3    Steele, J.L.4
  • 14
    • 0028982362 scopus 로고
    • Bacterial ectoenzymes in marine waters: Activity ratios and temperature responses in three oceanographic provinces
    • Christian, J. R., and D. M. Karl. 1995. Bacterial ectoenzymes in marine waters: activity ratios and temperature responses in three oceanographic provinces. Limnol. Oceanogr. 40:1042-1049.
    • (1995) Limnol. Oceanogr. , vol.40 , pp. 1042-1049
    • Christian, J.R.1    Karl, D.M.2
  • 16
    • 0034713903 scopus 로고    scopus 로고
    • Structural similarities and evolutionary relationships in chloride-dependent alpha-amylases
    • D'Amico, S., C. Gerday, and G. Feller. 2000. Structural similarities and evolutionary relationships in chloride-dependent alpha-amylases. Gene 253:95-105.
    • (2000) Gene , vol.253 , pp. 95-105
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 18
    • 0001847041 scopus 로고
    • Microbial exopolymer secretions in ocean environments: Their role(s) in food webs and marine processes
    • Decho, A. W. 1990. Microbial exopolymer secretions in ocean environments: their role(s) in food webs and marine processes. Oceanogr. Mar. Biol. Annu. Rev. 28:73-153.
    • (1990) Oceanogr. Mar. Biol. Annu. Rev. , vol.28 , pp. 73-153
    • Decho, A.W.1
  • 19
    • 0002685103 scopus 로고
    • Methods for the observation and use in feeding experiments of microbial exopolymers
    • P. F. Kemp, B. F. Sherr, E. B. Sherr, and J. J. Cole (ed.). Lewis Publishers, London, United Kingdom
    • Decho, A. W. 1993. Methods for the observation and use in feeding experiments of microbial exopolymers, p. 685-694. In P. F. Kemp, B. F. Sherr, E. B. Sherr, and J. J. Cole (ed.), Handbook of methods in aquatic microbial ecology. Lewis Publishers, London, United Kingdom.
    • (1993) Handbook of Methods in Aquatic Microbial Ecology , pp. 685-694
    • Decho, A.W.1
  • 20
    • 85024726292 scopus 로고
    • Isolation of an obligately barophilic bacterium and description of a new genus, Colwellia gen. nov.
    • Deming, J. W., L. K. Somers, W. L. Straube, D. G. Swartz, and M. T. MacDonell. 1988. Isolation of an obligately barophilic bacterium and description of a new genus, Colwellia gen. nov. Syst. Appl. Microbiol. 10:152-160.
    • (1988) Syst. Appl. Microbiol. , vol.10 , pp. 152-160
    • Deming, J.W.1    Somers, L.K.2    Straube, W.L.3    Swartz, D.G.4    MacDonell, M.T.5
  • 21
    • 0002555472 scopus 로고    scopus 로고
    • Search and discovery of microbial enzymes from thermally extreme environments in the ocean
    • R. P. Burns and R. P. Dick (ed.). Marcel Dekker, New York, N.Y.
    • Deming, J. W., and J. A. Baross. 2001. Search and discovery of microbial enzymes from thermally extreme environments in the ocean, p. 327-362. In R. P. Burns and R. P. Dick (ed.), Enzymes in the environment. Marcel Dekker, New York, N.Y.
    • (2001) Enzymes in the Environment , pp. 327-362
    • Deming, J.W.1    Baross, J.A.2
  • 22
    • 33749946901 scopus 로고
    • Colorimetric method of determination of sugars and related substances
    • Dubois, M., K. A. Gilles, J. K. Hamilton, P. A. Rebers, and F. Smith. 1956. Colorimetric method of determination of sugars and related substances. Anal. Chem. 18:350-356.
    • (1956) Anal. Chem. , vol.18 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 23
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and G. Begg. 1967. A protein sequenator. Eur. J. Biochem. 1:80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 25
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes
    • Fields, P. A., and G. N. Somero. 1998. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. USA 95:11476-11481.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 26
    • 0034973280 scopus 로고    scopus 로고
    • Review. Protein function at thermal extremes: Balancing stability and flexibility
    • Fields, P. A. 2001. Review. Protein function at thermal extremes: balancing stability and flexibility. Comp. Biochem. Physiol. A Comp. Physiol. 129:417-431.
    • (2001) Comp. Biochem. Physiol. A Comp. Physiol. , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 28
    • 0002791858 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase
    • S. Holgate and S.-E. Dahlen, (ed.). Marcel Dekker, New York, N.Y.
    • Haeggstrom, J. Z. 1998. Leukotriene A4 hydrolase, p. 51-76. In S. Holgate and S.-E. Dahlen, (ed.), 5-Lipoxygenase products in asthma. Marcel Dekker, New York, N.Y.
    • (1998) 5-Lipoxygenase Products in Asthma , pp. 51-76
    • Haeggstrom, J.Z.1
  • 29
    • 0034099760 scopus 로고    scopus 로고
    • Structure, function and regulation of leukotriene A4 hydrolase
    • Haeggstrom, J. Z. 2000. Structure, function and regulation of leukotriene A4 hydrolase. Am. J. Respir. Crit. Care Med. 161:S25-S31.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161
    • Haeggstrom, J.Z.1
  • 30
    • 0028993544 scopus 로고
    • Bacteria in sea ice and underlying water of the eastern Weddell Sea in midwinter
    • Helmke, E., and H. Weyland. 1995. Bacteria in sea ice and underlying water of the eastern Weddell Sea in midwinter. Mar. Ecol. Prog. Ser. 117:269-287.
    • (1995) Mar. Ecol. Prog. Ser. , vol.117 , pp. 269-287
    • Helmke, E.1    Weyland, H.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., J. Thompson, T. Gibson, J. D. Thompson, D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 32
    • 0016170446 scopus 로고
    • Metal substitutions and inhibition of thermolysin: Spectra of the cobalt enzyme
    • Holmquist, B., and Vallee, B. L. 1974. Metal substitutions and inhibition of thermolysin: spectra of the cobalt enzyme. J. Biol. Chem. 249:4601-4607.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4601-4607
    • Holmquist, B.1    Vallee, B.L.2
  • 33
    • 0034548849 scopus 로고    scopus 로고
    • Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice
    • Huston, A. L., B. B. Krieger-Brockett, and J. W. Deming. 2000. Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice. Environ. Microbiol. 2:383-388.
    • (2000) Environ. Microbiol. , vol.2 , pp. 383-388
    • Huston, A.L.1    Krieger-Brockett, B.B.2    Deming, J.W.3
  • 34
    • 0036034924 scopus 로고    scopus 로고
    • Relationships between microbial extracellular enzymatic activity and suspended and sinking particulate organic matter: Seasonal transformations in the North Water
    • Huston, A. L., and J. W. Deming. 2002. Relationships between microbial extracellular enzymatic activity and suspended and sinking particulate organic matter: seasonal transformations in the North Water. Deep-Sea Res. II 49:5211-5225.
    • (2002) Deep-Sea Res. II , vol.49 , pp. 5211-5225
    • Huston, A.L.1    Deming, J.W.2
  • 36
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai, A. 1980. Thermostability and aliphatic index of globular proteins. J. Biochem. 88:1895-1898.
    • (1980) J. Biochem. , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 37
    • 0034717156 scopus 로고    scopus 로고
    • Stability and stabilization of globular proteins in solution
    • Jaenicke, R. 2000. Stability and stabilization of globular proteins in solution. J. Biotechnol. 79:193-203.
    • (2000) J. Biotechnol. , vol.79 , pp. 193-203
    • Jaenicke, R.1
  • 38
    • 0036528499 scopus 로고    scopus 로고
    • Phylogenetic diversity of numerically important Arctic sea-ice bacteria cultured at subzero temperature
    • Junge, K., J. F. Imhoff, J. T. Staley, and J. W. Deming. 2002. Phylogenetic diversity of numerically important Arctic sea-ice bacteria cultured at subzero temperature. Microb. Ecol. 43:315-328.
    • (2002) Microb. Ecol. , vol.43 , pp. 315-328
    • Junge, K.1    Imhoff, J.F.2    Staley, J.T.3    Deming, J.W.4
  • 39
    • 0346037119 scopus 로고    scopus 로고
    • High concentrations of exopolymeric substances in Arctic winter sea ice: Implications for the polar ocean carbon cycle and cryoprotection of diatoms
    • Krembs, C., H. Eicken, K. Junge, and J. W. Deming. 2002. High concentrations of exopolymeric substances in Arctic winter sea ice: implications for the polar ocean carbon cycle and cryoprotection of diatoms. Deep-Sea Res. I 49:2163-2181.
    • (2002) Deep-Sea Res. I , vol.49 , pp. 2163-2181
    • Krembs, C.1    Eicken, H.2    Junge, K.3    Deming, J.W.4
  • 40
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 41
    • 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
  • 42
    • 0025806344 scopus 로고
    • Characterization of a metalloprotease from psychrophilic Xanthomonas maltophilia
    • Margesin, R., and F. Schinner. 1991. Characterization of a metalloprotease from psychrophilic Xanthomonas maltophilia. FEMS Microbiol. Lett. 79:257-262.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 257-262
    • Margesin, R.1    Schinner, F.2
  • 43
    • 0036035999 scopus 로고    scopus 로고
    • Viral and bacterial production in the North Water: In situ measurements, batch-culture experiments and characterization and distribution of a virus-host system
    • Middleboe, M., T. G. Nielson, and P. J. Bjornsen. 2002. Viral and bacterial production in the North Water: in situ measurements, batch-culture experiments and characterization and distribution of a virus-host system. Deep-Sea Res. II 49:5063-5079.
    • (2002) Deep-Sea Res. II , vol.49 , pp. 5063-5079
    • Middleboe, M.1    Nielson, T.G.2    Bjornsen, P.J.3
  • 45
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita, R. Y. 1975. Psychrophilic bacteria. Bacteriol. Rev. 39:144-167.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 46
    • 0031269842 scopus 로고    scopus 로고
    • Purification and characterization of a cold-active protease from psychrotrophic Serratia marcescens AP3801
    • Morita, Y., K. Kondo, Q. Hasan, T. Sakaguchi, Y. Murakami, J. Yokoyama, and E. Tamiya. 1997. Purification and characterization of a cold-active protease from psychrotrophic Serratia marcescens AP3801. J. Am. Oil Chem. Soc. 74:1377-1383.
    • (1997) J. Am. Oil Chem. Soc. , vol.74 , pp. 1377-1383
    • Morita, Y.1    Kondo, K.2    Hasan, Q.3    Sakaguchi, T.4    Murakami, Y.5    Yokoyama, J.6    Tamiya, E.7
  • 47
    • 0034736267 scopus 로고    scopus 로고
    • Distributions of structural features contributing to thermostability in mesophilic and thermophilic α/β barrel glycosyl hydrolases
    • Panasik, N., J. E. Brenchley, and G. K. Farber. 2000. Distributions of structural features contributing to thermostability in mesophilic and thermophilic α/β barrel glycosyl hydrolases. Biochim. Biophys. Acta 1543:189-201.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 189-201
    • Panasik, N.1    Brenchley, J.E.2    Farber, G.K.3
  • 48
    • 0035977796 scopus 로고    scopus 로고
    • Temperature and substrates as interactive limiting factors for marine heterotrophic bacteria
    • Pomeroy, L. R., and W. J. Wiebe. 2001. Temperature and substrates as interactive limiting factors for marine heterotrophic bacteria. Aquat. Microb. Ecol. 23:187-204.
    • (2001) Aquat. Microb. Ecol. , vol.23 , pp. 187-204
    • Pomeroy, L.R.1    Wiebe, W.J.2
  • 49
    • 0026720247 scopus 로고
    • Crystallin ribonuclease A loses function below the dynamical transition at 220 K
    • Rasmussen, B. F., A. M. Stock, D. Rings, and G. A. Petsko. 1992. Crystallin ribonuclease A loses function below the dynamical transition at 220 K. Nature 357:423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Rings, D.3    Petsko, G.A.4
  • 50
    • 0029088274 scopus 로고
    • Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174
    • Rattray, F. P., W. Bockelmann, and P. F. Fox. 1995. Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174. Appl. Environ. Microbiol. 61:3454-3456.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3454-3456
    • Rattray, F.P.1    Bockelmann, W.2    Fox, P.F.3
  • 51
    • 3342936478 scopus 로고    scopus 로고
    • A comprehensive analysis of 40 blind protein structure predictions
    • Samudrala, R., and M. Levitt. 2002. A comprehensive analysis of 40 blind protein structure predictions. BMC Struct. Biol. 2:3-18.
    • (2002) BMC Struct. Biol. , vol.2 , pp. 3-18
    • Samudrala, R.1    Levitt, M.2
  • 52
    • 0034731469 scopus 로고    scopus 로고
    • Approaches for deciphering the structural basis of low temperature enzyme activity
    • Sheridan, P. P., N. Panasik, J. M. Coombs, and J. E. Brenchley. 2000. Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta 1543:417-433.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 417-433
    • Sheridan, P.P.1    Panasik, N.2    Coombs, J.M.3    Brenchley, J.E.4
  • 53
    • 0026616183 scopus 로고
    • Intense hydrolytic enzyme activity on marine aggregates and implications for rapid particle dissolution
    • Smith, D. C., M. Simon, A. L. Alldredge, and F. Azam. 1992. Intense hydrolytic enzyme activity on marine aggregates and implications for rapid particle dissolution. Nature 359:139-142.
    • (1992) Nature , vol.359 , pp. 139-142
    • Smith, D.C.1    Simon, M.2    Alldredge, A.L.3    Azam, F.4
  • 55
    • 0002960761 scopus 로고
    • Stabilization of protein structures by solvents
    • T. E. Creighton (ed.). IRL Press, New York, N.Y.
    • Timasheff, S. N., and T. Arakawa. 1988. Stabilization of protein structures by solvents, p. 331-345. In T. E. Creighton (ed.), Protein structure, a practical approach. IRL Press, New York, N.Y.
    • (1988) Protein Structure, A Practical Approach , pp. 331-345
    • Timasheff, S.N.1    Arakawa, T.2
  • 56
    • 0001855948 scopus 로고
    • A physicochemical basis for the selection of osmolytes in nature
    • G. N. Somero, C. B. Osmond, and C. L. Bolis (ed.). Springer-Verlag, Berlin, Germany
    • Timasheff, S. N. 1992. A physicochemical basis for the selection of osmolytes in nature, p. 70-84. In G. N. Somero, C. B. Osmond, and C. L. Bolis (ed.), Water and life. Springer-Verlag, Berlin, Germany.
    • (1992) Water and Life , pp. 70-84
    • Timasheff, S.N.1
  • 57
    • 0028191250 scopus 로고
    • Extracellular enzyme activity in the Arctic northeast water polynya
    • Vetter, Y.-A., and J. W. Deming. 1994. Extracellular enzyme activity in the Arctic northeast water polynya. Mar. Ecol. Prog. Ser. 114:23-34.
    • (1994) Mar. Ecol. Prog. Ser. , vol.114 , pp. 23-34
    • Vetter, Y.-A.1    Deming, J.W.2
  • 58
    • 0031840704 scopus 로고    scopus 로고
    • A predictive model of bacterial foraging by means of freely released extracellular enzymes
    • Vetter, Y. A., J. W. Deming, P. A. Jumars, and B. B. Krieger-Brockett. 1998. A predictive model of bacterial foraging by means of freely released extracellular enzymes. Microb. Ecol. 36:75-92.
    • (1998) Microb. Ecol. , vol.36 , pp. 75-92
    • Vetter, Y.A.1    Deming, J.W.2    Jumars, P.A.3    Krieger-Brockett, B.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.