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Volumn 255, Issue 3, 1998, Pages 638-646

The third, serine proteinase with chymotrypsin specificity isolated from Atlantic cod (Gadus morhua) is a type-II elastase

Author keywords

Amino acid sequence; Atlantic cod; Cold adaptation; Elastase; Serine protease

Indexed keywords

CHYMOTRYPSIN; ELASTASE; SERINE PROTEINASE;

EID: 0032146248     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550638.x     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 0001872730 scopus 로고
    • Elastases: Structure, function and pathological role
    • Bieth, J. (1978) Elastases: Structure, function and pathological role, Front. Matrix Biol. 6, 1-82.
    • (1978) Front. Matrix Biol. , vol.6 , pp. 1-82
    • Bieth, J.1
  • 2
    • 0010586561 scopus 로고
    • Pancreatic elastase: Purification, properties, and function
    • Lewis, U. J., Williams, D. E. & Brink, N. G. (1956) Pancreatic elastase: Purification, properties, and function, J. Biol. Chem. 222, 705-720.
    • (1956) J. Biol. Chem. , vol.222 , pp. 705-720
    • Lewis, U.J.1    Williams, D.E.2    Brink, N.G.3
  • 3
    • 77956999337 scopus 로고
    • (Colowick, S. P. & Kaplan, N. O., eds) Academic Press, New York
    • Shotton, D. M. (1970) in Methods in enzymology (Colowick, S. P. & Kaplan, N. O., eds) vol. 19, pp. 113-140, Academic Press, New York.
    • (1970) Methods in Enzymology , vol.19 , pp. 113-140
    • Shotton, D.M.1
  • 4
    • 0016692253 scopus 로고
    • Physical parameters and chemical composition of porcine pancreatic elastase II
    • Ardelt, W. (1975) Physical parameters and chemical composition of porcine pancreatic elastase II, Biochim. Biophys. Acta 393, 267-273.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 267-273
    • Ardelt, W.1
  • 5
    • 0017641735 scopus 로고
    • Purification and characterization of porcine elastase II and investigation of its elastolytic specificity
    • Gertler, A., Weiss, Y. & Burstein, Y. (1977) Purification and characterization of porcine elastase II and investigation of its elastolytic specificity, Biochemistry 16, 2709-2716.
    • (1977) Biochemistry , vol.16 , pp. 2709-2716
    • Gertler, A.1    Weiss, Y.2    Burstein, Y.3
  • 6
    • 0016670936 scopus 로고
    • Human pancreatic enzymes: Purification and characterization of a non-elastolytic enzyme, protease E. resembling elastase
    • Mallory, P. A. & Travis, J. (1975) Human pancreatic enzymes: purification and characterization of a non-elastolytic enzyme, protease E. resembling elastase, Biochemistry 14, 722-730.
    • (1975) Biochemistry , vol.14 , pp. 722-730
    • Mallory, P.A.1    Travis, J.2
  • 7
    • 0017174488 scopus 로고
    • Purification and characterization of two human pancreatic elastases
    • Largman, C., Brodrick, J. W. & Geokas, M. C. (1976) Purification and characterization of two human pancreatic elastases, Biochemistry 15, 2491-2500.
    • (1976) Biochemistry , vol.15 , pp. 2491-2500
    • Largman, C.1    Brodrick, J.W.2    Geokas, M.C.3
  • 9
    • 0020484805 scopus 로고
    • Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequence
    • MacDonald, R. J., Swift, G. H., Quinto, C., Swain, W., Pictet, R. L., Nikovits, W. & Rutter, W. J. (1982) Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequence, Biochemistry 21, 1453-1463.
    • (1982) Biochemistry , vol.21 , pp. 1453-1463
    • MacDonald, R.J.1    Swift, G.H.2    Quinto, C.3    Swain, W.4    Pictet, R.L.5    Nikovits, W.6    Rutter, W.J.7
  • 10
    • 0020546301 scopus 로고
    • Isolation and characterization of rat pancreatic elastase
    • Largman, C. (1983) Isolation and characterization of rat pancreatic elastase, Biochemistry 22, 3763-3770.
    • (1983) Biochemistry , vol.22 , pp. 3763-3770
    • Largman, C.1
  • 11
    • 0029148529 scopus 로고
    • Purification, characterization and substrate specificity of rat pancreatic elastase II
    • Szilagyi, C. M., Sarfati, P., Pradayrol, L. & Morisset, J. (1995) Purification, characterization and substrate specificity of rat pancreatic elastase II, Biochim. Biophys. Acta 1251, 55-65.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 55-65
    • Szilagyi, C.M.1    Sarfati, P.2    Pradayrol, L.3    Morisset, J.4
  • 12
    • 0016220144 scopus 로고
    • Isolation and amino-terminal sequence analysis of two dissimilar pancreatic proelastases from the African lungfish
    • DeHaën, C. & Gertler, A. (1974) Isolation and amino-terminal sequence analysis of two dissimilar pancreatic proelastases from the African lungfish, Biochemistry 13, 2673-2677.
    • (1974) Biochemistry , vol.13 , pp. 2673-2677
    • DeHaën, C.1    Gertler, A.2
  • 13
    • 0001092869 scopus 로고
    • Pancreatic proteolytic enzymes from carp (Cyprinus carpio) - II. Kinetic properties and inhibition studies of trypsin, chymotrypsin and elastase
    • Cohen, T., Gertler, A. & Birk, Y. (1981) Pancreatic proteolytic enzymes from carp (Cyprinus carpio) - II. Kinetic properties and inhibition studies of trypsin, chymotrypsin and elastase, Comp. Biochem. Physiol. 69B, 647-653.
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 647-653
    • Cohen, T.1    Gertler, A.2    Birk, Y.3
  • 14
    • 46549101942 scopus 로고
    • Distribution of pancreatic elastase and metalloproteinase in several species of fish
    • Yoshinaka, R., Sato, M., Tanaka, H. & Ikeda, S. (1985) Distribution of pancreatic elastase and metalloproteinase in several species of fish, Comp. Biochem. Physiol. 80B, 227-233.
    • (1985) Comp. Biochem. Physiol. , vol.80 B , pp. 227-233
    • Yoshinaka, R.1    Sato, M.2    Tanaka, H.3    Ikeda, S.4
  • 15
    • 0024352698 scopus 로고
    • Purification and characterization of chymotrypsin, trypsin and elastase like proteinases from cod (Gadus morhua L.)
    • Raae, A. J. & Walther, B. T. (1989) Purification and characterization of chymotrypsin, trypsin and elastase like proteinases from cod (Gadus morhua L.), Comp. Biochem. Physiol. 93B, 317-324.
    • (1989) Comp. Biochem. Physiol. , vol.93 B , pp. 317-324
    • Raae, A.J.1    Walther, B.T.2
  • 16
    • 0025645990 scopus 로고
    • Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua)
    • Gildberg, A. & Øverbø, K. (1990) Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua), Comp. Biochem. Physiol. 97B, 775-782.
    • (1990) Comp. Biochem. Physiol. , vol.97 B , pp. 775-782
    • Gildberg, A.1    Øverbø, K.2
  • 17
    • 0027194992 scopus 로고
    • Properties of elastase from Atlantic cod, a cold-adapted proteinase
    • Ásgeirsson, B. & Bjarnason, J. B. (1993) Properties of elastase from Atlantic cod, a cold-adapted proteinase, Biochim. Biophys. Acta 1164, 91-100.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 91-100
    • Ásgeirsson, B.1    Bjarnason, J.B.2
  • 18
    • 0027282004 scopus 로고
    • Purification and characterization of elastase from the pyloric caeca of Rainbow trout (Oncorhynchus mykiss)
    • Bassompierre, M., Nielsen, H. H. & Børresen, T. (1993) Purification and characterization of elastase from the pyloric caeca of Rainbow trout (Oncorhynchus mykiss), Comp. Biochem. Physiol. 106B, 331-336.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 331-336
    • Bassompierre, M.1    Nielsen, H.H.2    Børresen, T.3
  • 19
    • 7344224219 scopus 로고
    • Doctoral Thesis, University of Tromso, Norway
    • Berglund, G. I. (1995) Doctoral Thesis, University of Tromso, Norway.
    • (1995)
    • Berglund, G.I.1
  • 20
    • 0030924747 scopus 로고    scopus 로고
    • Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta
    • Aittaleb, M., Hubner, R., Lamottebrasseur, J. & Gerday, C. (1997) Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta, Protein Eng. 10, 475-477.
    • (1997) Protein Eng. , vol.10 , pp. 475-477
    • Aittaleb, M.1    Hubner, R.2    Lamottebrasseur, J.3    Gerday, C.4
  • 21
    • 85008034260 scopus 로고
    • Purification and some properties of elastase from the pancreas of catfish
    • Yoshinaka, R., Tanaka, H., Sato, M. & Ikeda, S. (1982) Purification and some properties of elastase from the pancreas of catfish, Bull. Jap. Soc. Sci. Fish. 48, 573-579.
    • (1982) Bull. Jap. Soc. Sci. Fish. , vol.48 , pp. 573-579
    • Yoshinaka, R.1    Tanaka, H.2    Sato, M.3    Ikeda, S.4
  • 22
    • 0025761645 scopus 로고
    • Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin
    • Ásgeirsson, B. & Bjarnason, J. B. (1991) Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin, Comp. Biochem. Physiol. 99B, 327-335.
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 327-335
    • Ásgeirsson, B.1    Bjarnason, J.B.2
  • 25
    • 0016363174 scopus 로고
    • The synthesis and analytical use of a highly sensitive and convenient substrate of elastase
    • Bieth, J. G., Spiess, B. & Wermuth, C. G. (1974) The synthesis and analytical use of a highly sensitive and convenient substrate of elastase, Biochem. Med. 11, 350-357.
    • (1974) Biochem. Med. , vol.11 , pp. 350-357
    • Bieth, J.G.1    Spiess, B.2    Wermuth, C.G.3
  • 26
    • 84935649647 scopus 로고
    • (Bergmeyer, H. U., ed.) Academic Press Inc., New York
    • Apple, W. (1974) in Methods of enzymatic analysis (Bergmeyer, H. U., ed.) vol. 2, pp. 1041-1045, Academic Press Inc., New York.
    • (1974) Methods of Enzymatic Analysis , vol.2 , pp. 1041-1045
    • Apple, W.1
  • 27
    • 0018627098 scopus 로고
    • Quantitation of proteins solubilized in sodium dodecyl sulfate-mercaptoethanol-tris electrophoresis buffer
    • Zaman, Z. & Verwilghen, R. L. (1979) Quantitation of proteins solubilized in sodium dodecyl sulfate-mercaptoethanol-tris electrophoresis buffer, Anal. Biochem. 100, 64-69.
    • (1979) Anal. Biochem. , vol.100 , pp. 64-69
    • Zaman, Z.1    Verwilghen, R.L.2
  • 28
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2424.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2424
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 31
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J. & Craik, C. S. (1995) Structural basis of substrate specificity in the serine proteases, Protein Sci. 4, 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 32
    • 0028892730 scopus 로고
    • Chymotrypsin isoenzymes in Atlantic cod: Differences in kinetics and substrate specificity
    • Raae, A. J., Flengsrud, R. & Sletten, K. (1995) Chymotrypsin isoenzymes in Atlantic cod: differences in kinetics and substrate specificity, Comp. Biochem. Physiol. 112B, 393-398.
    • (1995) Comp. Biochem. Physiol. , vol.112 B , pp. 393-398
    • Raae, A.J.1    Elengsrud, R.2    Sletten, K.3
  • 33
    • 0015244383 scopus 로고
    • Inhibition of porcine elastase by turkey ovomucoid and chicken ovoinhibitor
    • Gertler, A. & Feinstein, G. (1971) Inhibition of porcine elastase by turkey ovomucoid and chicken ovoinhibitor, Eur. J. Biochem. 20, 547-552.
    • (1971) Eur. J. Biochem. , vol.20 , pp. 547-552
    • Gertler, A.1    Feinstein, G.2
  • 34
    • 0017063195 scopus 로고
    • The inhibition of human leukocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin
    • Feinstein, G., Malemud, C. J. & Janoff, A. (1976) The inhibition of human leukocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin, Biochim. Biophys. Acta 429, 925-932.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 925-932
    • Feinstein, G.1    Malemud, C.J.2    Janoff, A.3
  • 35
    • 0001820118 scopus 로고
    • (Colowick, S. P. & Kaplan, N. O., eds) Academic Press, New York
    • Wilcox, P. E. (1970) in Methods in enzymology (Colowick, S. P. & Kaplan, N. O., eds) vol. 19, pp. 64-108, Academic Press, New York.
    • (1970) Methods in Enzymology , vol.19 , pp. 64-108
    • Wilcox, P.E.1
  • 37
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings, N. D. & Barrett, A. J. (1993) Evolutionary families of peptidases, Biochem. J. 290, 205-218.
    • (1993) Biochem. J. , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 38
    • 0023855495 scopus 로고
    • Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic cloning
    • Tani, T., Ohsumi, J., Mita, K. & Takiguchi, Y. (1988) Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic cloning, J. Biol. Chem. 263, 1231-1239.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1231-1239
    • Tani, T.1    Ohsumi, J.2    Mita, K.3    Takiguchi, Y.4
  • 39
    • 0017160779 scopus 로고
    • p-Nitroanilides of 3-carboxypropionyl-peptides. Their cleavage by elastase, trypsin and chymotrypsin
    • Kasafirek, E., Fric, P., Slaby, J. & Malis, F. (1976) p-Nitroanilides of 3-carboxypropionyl-peptides. Their cleavage by elastase, trypsin and chymotrypsin, Eur. J. Biochem, 69, 1-13.
    • (1976) Eur. J. Biochem , vol.69 , pp. 1-13
    • Kasafirek, E.1    Fric, P.2    Slaby, J.3    Malis, F.4
  • 40
    • 0028955809 scopus 로고
    • Characterization of a collagenolytic serine proteinase from the Atlantic cod (Gadus morhua)
    • Kristjánsson, M. M., Gudmundsdóttir, S., Fox, J. W. & Bjarnason, J. B. (1995) Characterization of a collagenolytic serine proteinase from the Atlantic cod (Gadus morhua), Comp. Biochem. Physiol. 110B, 707-717.
    • (1995) Comp. Biochem. Physiol. , vol.110 B , pp. 707-717
    • Kristjánsson, M.M.1    Gudmundsdóttir, S.2    Fox, J.W.3    Bjarnason, J.B.4
  • 41
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M. & Kato, I. (1980) Protein inhibitors of proteinases, Annu. Rev. Biochem. 49, 593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 43
    • 0025525188 scopus 로고
    • Cold adaptation in marine organisms
    • Johnston, I. A. (1990) Cold adaptation in marine organisms, Phil. Trans. R. Soc. Lond. B 326, 655-667.
    • (1990) Phil. Trans. R. Soc. Lond. B , vol.326 , pp. 655-667
    • Johnston, I.A.1
  • 44
    • 0025716254 scopus 로고
    • Protein structure and function at low temperatures
    • Jaenicke, R. (1990) Protein structure and function at low temperatures, Phil. Trans. R. Soc. Lond. B 326, 535-553.
    • (1990) Phil. Trans. R. Soc. Lond. B , vol.326 , pp. 535-553
    • Jaenicke, R.1
  • 45
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, charaterization and sequence of the heatlabile subtilisin from the Antartic psychrophile Bacillus TA41
    • Davail, S., Feller, G., Narinx, E. & Gerdy, C. (1994) Cold adaptation of proteins. Purification, charaterization and sequence of the heatlabile subtilisin from the Antartic psychrophile Bacillus TA41, J. Biol. Chem. 269, 17 448-17 453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerdy, C.4
  • 46
    • 0029042854 scopus 로고
    • Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution
    • Heimstad, E. S., Hansen, L. K. & Smaläs, A. O. (1995) Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution, Protein Eng. 8, 379-388.
    • (1995) Protein Eng. , vol.8 , pp. 379-388
    • Heimstad, E.S.1    Hansen, L.K.2    Smaläs, A.O.3


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