메뉴 건너뛰기




Volumn 159, Issue 3-4, 1998, Pages 203-216

Purification and characterization of several digestive proteases from the blue abalone, Haliotis fulgens

Author keywords

Abalone; Carboxypeptidase; Haliotis fulgens; Serine like proteases

Indexed keywords

HALIOTIDAE; HALIOTIS FULGENS;

EID: 0001025895     PISSN: 00448486     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0044-8486(97)00172-5     Document Type: Article
Times cited : (21)

References (35)
  • 2
    • 85030557278 scopus 로고
    • Enzyme Handbook, Springer-Verlag, New York
    • Barman, T.E. (Ed.), 1969. Enzyme Handbook, Vol III. Springer-Verlag, New York, pp. 1–928.
    • (1969) , pp. 1-928
    • Barman, T.E.1
  • 3
    • 0024791521 scopus 로고
    • Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing-active site geometry, ion pairs and solvent structure
    • Bartunik, H.D, Summers, L.J, Bartsch, H.H, Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing-active site geometry, ion pairs and solvent structure. J. Mol. Biol. 210 (1989), 813–828.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 4
    • 0027534408 scopus 로고
    • Purification and autolytic degradation of a calpain-like calcium-dependent proteinase from lobster (Homarus americanus) striated muscle
    • Beyette, J.R, Ma, J.-S, Mykles, D.L, Purification and autolytic degradation of a calpain-like calcium-dependent proteinase from lobster (Homarus americanus) striated muscle. Comp. Biochem. Physiol. 104B (1993), 95–99.
    • (1993) Comp. Biochem. Physiol. , vol.104B , pp. 95-99
    • Beyette, J.R.1    Ma, J.-S.2    Mykles, D.L.3
  • 5
    • 84986431478 scopus 로고
    • Purification and characterization of proteases from the viscera of milkfish (Chanos chanos)
    • Chen, C.S, Tsao, C.Y, Jiang, S.T, Purification and characterization of proteases from the viscera of milkfish (Chanos chanos). J. Food Biochem. 12 (1988), 269–288.
    • (1988) J. Food Biochem. , vol.12 , pp. 269-288
    • Chen, C.S.1    Tsao, C.Y.2    Jiang, S.T.3
  • 6
    • 0000733607 scopus 로고
    • Proteolytic activity of the crude enzyme extracted from the digestive tract of marine gastropods
    • Cho, D.M, Pyeun, J.H, Byun, D.S, Kim, C.Y, Proteolytic activity of the crude enzyme extracted from the digestive tract of marine gastropods. Bull. Korean Fish. Soc. 16 (1983), 216–224.
    • (1983) Bull. Korean Fish. Soc. , vol.16 , pp. 216-224
    • Cho, D.M.1    Pyeun, J.H.2    Byun, D.S.3    Kim, C.Y.4
  • 7
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L.A, Curtis, J.W, Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155 (1986), 155–167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Curtis, J.W.2
  • 8
    • 0003469198 scopus 로고
    • Plant proteolytic enzymes, Vol. CRC Press, Boca Raton, FL,.
    • Dalling, M.J., 1986. Plant proteolytic enzymes, Vol. 1. CRC Press, Boca Raton, FL, pp. 475–530.
    • (1986) , vol.1 , pp. 475-530
    • Dalling, M.J.1
  • 10
    • 33751157824 scopus 로고
    • Enzymes with peptidase and proteinase activity from the digestive systems of a freshwater and marine decapod
    • Garcı́a-Carreño, F.L, Enzymes with peptidase and proteinase activity from the digestive systems of a freshwater and marine decapod. J. Agric. Food Chem. 42 (1994), 1456–1461.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1456-1461
    • Garcı́a-Carreño, F.L.1
  • 11
    • 0014603717 scopus 로고
    • Isolation and comparative properties of shrimp trypsin
    • Gates, B.J, Travis, J, Isolation and comparative properties of shrimp trypsin. Biochemistry 8 (1969), 4483–4489.
    • (1969) Biochemistry , vol.8 , pp. 4483-4489
    • Gates, B.J.1    Travis, J.2
  • 12
    • 0025645990 scopus 로고
    • Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua)
    • Gildberg, A, Øverbø, K, Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua). Comp. Biochem. Physiol. 97B (1990), 775–782.
    • (1990) Comp. Biochem. Physiol. , vol.97B , pp. 775-782
    • Gildberg, A.1    Øverbø, K.2
  • 13
    • 0028113999 scopus 로고
    • Comparative and optimized dabsyl-amino acid analysis of synthetic phosphopeptides and glycopeptides
    • Gorbics, L, Urge, L, Otvos, L, Comparative and optimized dabsyl-amino acid analysis of synthetic phosphopeptides and glycopeptides. J. Chromatogr. A 676 (1994), 169–176.
    • (1994) J. Chromatogr. A , vol.676 , pp. 169-176
    • Gorbics, L.1    Urge, L.2    Otvos, L.3
  • 14
    • 0016670373 scopus 로고
    • The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships
    • Haën, C, Neurath, H, Teller, D.C, The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships. J. Mol. Biol. 92 (1975), 225–259.
    • (1975) J. Mol. Biol. , vol.92 , pp. 225-259
    • Haën, C.1    Neurath, H.2    Teller, D.C.3
  • 15
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey, J.P, Johnson, W.C, Information content in the circular dichroism of proteins. Biochemistry 20 (1981), 1085–1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey, J.P.1    Johnson, W.C.2
  • 17
    • 0028031778 scopus 로고
    • Enzymatic properties of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii
    • Kim, H.R, Meyers, S.P, Pyeun, J.H, Godber, J.S, Enzymatic properties of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii. Comp. Biochem. Physiol. 107B (1994), 197–203.
    • (1994) Comp. Biochem. Physiol. , vol.107B , pp. 197-203
    • Kim, H.R.1    Meyers, S.P.2    Pyeun, J.H.3    Godber, J.S.4
  • 18
    • 0026567107 scopus 로고
    • Purification and characterization of two chymotrypsin-like proteases from the pyloric caeca of rainbow trout (Oncorhynchus mykiss)
    • Kristjánsson, M.M, Nielsen, H.H, Purification and characterization of two chymotrypsin-like proteases from the pyloric caeca of rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. 101 (1992), 247–253.
    • (1992) Comp. Biochem. Physiol. , vol.101 , pp. 247-253
    • Kristjánsson, M.M.1    Nielsen, H.H.2
  • 19
    • 36849156983 scopus 로고
    • Sensitivity of circular dichroism to protein tertiary structure class
    • Manavalan, P, Johnson, W.C, Sensitivity of circular dichroism to protein tertiary structure class. Nature 305 (1983), 831–832.
    • (1983) Nature , vol.305 , pp. 831-832
    • Manavalan, P.1    Johnson, W.C.2
  • 20
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with coomassie blue dyes in polyacrylamide gels: systematic analysis
    • Neuhoff, V, Stamm, R, Eibl, H, Clear background and highly sensitive protein staining with coomassie blue dyes in polyacrylamide gels: systematic analysis. Electrophoresis 6 (1985), 427–448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 21
    • 0000359399 scopus 로고
    • On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia superba
    • Osnes, K.K, Mohr, V, On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia superba. Comp. Biochem. Physiol. 82B (1985), 607–619.
    • (1985) Comp. Biochem. Physiol. , vol.82B , pp. 607-619
    • Osnes, K.K.1    Mohr, V.2
  • 22
    • 0000608807 scopus 로고
    • Bovine procarboxypeptidase and carboxypeptidase A
    • In: Perlmann, G.E., Lorand, L. (Eds.),. Academic Press, New York
    • Pitra, P.H., 1970. Bovine procarboxypeptidase and carboxypeptidase A. In: Perlmann, G.E., Lorand, L. (Eds.), Methods Enzymol., Vol. 19. Academic Press, New York, pp. 460–503.
    • (1970) Methods Enzymol. , vol.19 , pp. 460-503
    • Pitra, P.H.1
  • 23
    • 0024352698 scopus 로고
    • Purification and characterization of chymotrypsin, trypsin and elastase like proteinases from cod (Gadus morhua L.)
    • Raae, A.J, Walther, B.T, Purification and characterization of chymotrypsin, trypsin and elastase like proteinases from cod (Gadus morhua L.). Comp. Biochem. Physiol. 93B (1989), 317–324.
    • (1989) Comp. Biochem. Physiol. , vol.93B , pp. 317-324
    • Raae, A.J.1    Walther, B.T.2
  • 24
    • 0014319582 scopus 로고
    • A new ultrasensitive method for the determination of proteolytic activity
    • Rinderknecht, H, Geokas, M.C, Silverman, P, Haverback, B.J, A new ultrasensitive method for the determination of proteolytic activity. Clin. Chim. Acta 21 (1968), 197–203.
    • (1968) Clin. Chim. Acta , vol.21 , pp. 197-203
    • Rinderknecht, H.1    Geokas, M.C.2    Silverman, P.3    Haverback, B.J.4
  • 25
    • 0016751788 scopus 로고
    • Isolation and characterization of papaya peptidase A from commercial chymopapain
    • Robinson, G.W, Isolation and characterization of papaya peptidase A from commercial chymopapain. Biochemistry 14 (1975), 3695–3700.
    • (1975) Biochemistry , vol.14 , pp. 3695-3700
    • Robinson, G.W.1
  • 29
    • 0021300884 scopus 로고
    • The metallobiochemistry of zinc enzymes
    • In: Meister, A. (Ed.), Adv. Enzymol., Vol. 56. Wiley,.
    • Valee, B.L., Galdes, A., 1984. The metallobiochemistry of zinc enzymes. In: Meister, A. (Ed.), Adv. Enzymol., Vol. 56. Wiley, pp. 283–430.
    • (1984) , pp. 283-430
    • Valee, B.L.1    Galdes, A.2
  • 30
    • 5744235228 scopus 로고
    • Trypsinogens and trypsins of various species
    • In: Perlmann, G.E., Lorand, L. (Eds.), Meth. Enzymol., Vol. 19. Academic Press, New York,.
    • Walsh, K.A., 1970. Trypsinogens and trypsins of various species. In: Perlmann, G.E., Lorand, L. (Eds.), Meth. Enzymol., Vol. 19. Academic Press, New York, pp. 41–63.
    • (1970) , pp. 41-63
    • Walsh, K.A.1
  • 31
    • 77957016166 scopus 로고
    • Serine proteases
    • In: Perlmann, G.E., Lorand, L. (Eds.), Meth. Enzymol., Academic Press, Vol. 19. New York,.
    • Walsh, K.A., Wilcox, P.E., 1970. Serine proteases. In: Perlmann, G.E., Lorand, L. (Eds.), Meth. Enzymol., Academic Press, Vol. 19. New York, pp. 31–111.
    • (1970) , pp. 31-111
    • Walsh, K.A.1    Wilcox, P.E.2
  • 32
    • 0001192303 scopus 로고
    • Kinetics of papain-catalyzed hydrolysis of alfa-N-benzoyl-L-arginine ethyl ester and alfa-N-benzoyl-L-argininamide
    • Whitaker, J.R, Bender, M.L, Kinetics of papain-catalyzed hydrolysis of alfa-N-benzoyl-L-arginine ethyl ester and alfa-N-benzoyl-L-argininamide. J. Am. Chem. Soc. 87 (1965), 2728–2737.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2728-2737
    • Whitaker, J.R.1    Bender, M.L.2
  • 33
    • 0014961122 scopus 로고
    • Purification and properties of a trypsin-like enzyme from the starfish Evasterias trochelii
    • Winter, W.P, Neurath, H, Purification and properties of a trypsin-like enzyme from the starfish Evasterias trochelii. Biochemistry 9 (1970), 4673–4679.
    • (1970) Biochemistry , vol.9 , pp. 4673-4679
    • Winter, W.P.1    Neurath, H.2
  • 34
    • 0014682668 scopus 로고
    • Structure of Subtilisin BPN′ at 2.5 Å resolution
    • Wright, C.S, Alden, R.A, Kraut, J, Structure of Subtilisin BPN′ at 2.5 Å resolution. Nature 221 (1969), 235–242.
    • (1969) Nature , vol.221 , pp. 235-242
    • Wright, C.S.1    Alden, R.A.2    Kraut, J.3
  • 35
    • 77957083353 scopus 로고
    • Invertebrate proteases
    • In: Lorand, L. (Ed.), Meth. Enzymol., Vol. 80. Academic Press, New York,.
    • Zwilling, R., Neurath, H., 1981. Invertebrate proteases. In: Lorand, L. (Ed.), Meth. Enzymol., Vol. 80. Academic Press, New York, pp. 633–664.
    • (1981) , pp. 633-664
    • Zwilling, R.1    Neurath, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.