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Volumn 112, Issue 2, 2009, Pages 442-447

Identification of a cysteine proteinase from Jumbo squid (Dosidicus gigas) hepatopancreas as cathepsin L

Author keywords

Cathepsin L; Cysteine proteinase; Jumbo squid

Indexed keywords

AMMONIUM SULFATE; ASPARTATE PROTEINASE INHIBITOR; CATHEPSIN B; CATHEPSIN H; CATHEPSIN L; CYSTEINE PROTEINASE; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR;

EID: 47949130997     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.05.100     Document Type: Article
Times cited : (32)

References (47)
  • 3
    • 0031418385 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin L from hepatopancreas of Carp Cyprinus carpio
    • Aranishi F., Ogata H., Hara K., Osatomi K., and Ishihara T. Purification and characterization of cathepsin L from hepatopancreas of Carp Cyprinus carpio. Comparative Biochemistry & Physiology 118B 3 (1997) 531-537
    • (1997) Comparative Biochemistry & Physiology , vol.118 B , Issue.3 , pp. 531-537
    • Aranishi, F.1    Ogata, H.2    Hara, K.3    Osatomi, K.4    Ishihara, T.5
  • 5
    • 0001132997 scopus 로고
    • Feeding and digestion in cephalopods
    • Saleuddin A.S.M., and Wilbur K.M. (Eds), Academic Press, New York
    • Boucad-Camou E., and Boucher-Rodhoni R. Feeding and digestion in cephalopods. In: Saleuddin A.S.M., and Wilbur K.M. (Eds). Physiology, Part 2 Vol. 5 (1983), Academic Press, New York 149-187
    • (1983) Physiology, Part 2 , vol.5 , pp. 149-187
    • Boucad-Camou, E.1    Boucher-Rodhoni, R.2
  • 6
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0035130633 scopus 로고    scopus 로고
    • Characterization of a novel heterodimeric cathepsin L-like protease and cDNA encoding the catalytic subunit of the protease in embryos of Artemia franciscana
    • Butler A.M., Alton A.L., and Warner A.H. Characterization of a novel heterodimeric cathepsin L-like protease and cDNA encoding the catalytic subunit of the protease in embryos of Artemia franciscana. Biochemistry Cell Biology 79 (2001) 43-56
    • (2001) Biochemistry Cell Biology , vol.79 , pp. 43-56
    • Butler, A.M.1    Alton, A.L.2    Warner, A.H.3
  • 8
    • 22544479434 scopus 로고    scopus 로고
    • Cysteine protease activity in Jumbo squid (Dosidicus gigas) hepatopancreas extracts
    • Cardenas-Lopez J.L., and Haard N.F. Cysteine protease activity in Jumbo squid (Dosidicus gigas) hepatopancreas extracts. Journal of Food Biochemistry 29 2 (2005) 171-186
    • (2005) Journal of Food Biochemistry , vol.29 , Issue.2 , pp. 171-186
    • Cardenas-Lopez, J.L.1    Haard, N.F.2
  • 9
    • 0023908317 scopus 로고
    • Delineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content
    • Dufour E., Dive V., and Toma F. Delineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content. Biochimica Biophysica Acta 955 (1988) 58-64
    • (1988) Biochimica Biophysica Acta , vol.955 , pp. 58-64
    • Dufour, E.1    Dive, V.2    Toma, F.3
  • 11
    • 0030492915 scopus 로고    scopus 로고
    • Influence of wound injury on accumulation of proteinase inhibitors in leaf and stem tissues of two processing tomato cultivars
    • El-Shamei Z., Wu J.W., and Haard N.F. Influence of wound injury on accumulation of proteinase inhibitors in leaf and stem tissues of two processing tomato cultivars. Journal of Food Biochemistry 20 (1996) 155-171
    • (1996) Journal of Food Biochemistry , vol.20 , pp. 155-171
    • El-Shamei, Z.1    Wu, J.W.2    Haard, N.F.3
  • 12
    • 0024256915 scopus 로고
    • Aspartic proteinases in fishes and aquatic invertebrates
    • Gildberg A. Aspartic proteinases in fishes and aquatic invertebrates. Comparative Biochemistry & Physiology 91B 3 (1988) 425-435
    • (1988) Comparative Biochemistry & Physiology , vol.91 B , Issue.3 , pp. 425-435
    • Gildberg, A.1
  • 14
    • 0001568343 scopus 로고    scopus 로고
    • Comparison of protease activity in liver among several species of squid and cuttlefish
    • Hatate H., Tanaka R., Suzuki N., and Hama Y. Comparison of protease activity in liver among several species of squid and cuttlefish. Fisheries Science 66 1 (2000) 182-183
    • (2000) Fisheries Science , vol.66 , Issue.1 , pp. 182-183
    • Hatate, H.1    Tanaka, R.2    Suzuki, N.3    Hama, Y.4
  • 15
    • 0031418662 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin L-like enzyme from the muscle of anchovy, Engraulis japonica
    • Heu M.S., Kim R.S., Cho D.M., Godber J.S., and Pyeun J.H. Purification and characterization of cathepsin L-like enzyme from the muscle of anchovy, Engraulis japonica. Comparative Biochemistry & Physiology 118B 3 (1997) 523-529
    • (1997) Comparative Biochemistry & Physiology , vol.118 B , Issue.3 , pp. 523-529
    • Heu, M.S.1    Kim, R.S.2    Cho, D.M.3    Godber, J.S.4    Pyeun, J.H.5
  • 17
    • 84986492795 scopus 로고
    • Effect of squid liver extract on proteins and on the texture of cooked squid mantle
    • Kolodziejska I., Pacana J., and Sikorski Z.E. Effect of squid liver extract on proteins and on the texture of cooked squid mantle. Journal of Food Biochemistry 16 3 (1992) 141-150
    • (1992) Journal of Food Biochemistry , vol.16 , Issue.3 , pp. 141-150
    • Kolodziejska, I.1    Pacana, J.2    Sikorski, Z.E.3
  • 18
    • 0028038829 scopus 로고
    • Proteolytic activity of crude enzyme extracts of squid Illex-Argentinus liver
    • Kolodziejska I., Szyc E., Karamac M., and Sikorski Z.E. Proteolytic activity of crude enzyme extracts of squid Illex-Argentinus liver. Journal of Food Biochemistry 18 1 (1994) 43-53
    • (1994) Journal of Food Biochemistry , vol.18 , Issue.1 , pp. 43-53
    • Kolodziejska, I.1    Szyc, E.2    Karamac, M.3    Sikorski, Z.E.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 77957773738 scopus 로고
    • Purification and characterization of proteinases identified as cathepsin L and L-like (58KDa) proteinase from mackarel (Scomber australasicus)
    • Lee J.J., Chen H.C., and Jiang S.T. Purification and characterization of proteinases identified as cathepsin L and L-like (58KDa) proteinase from mackarel (Scomber australasicus). Bioscience Biotechnology Biochemistry 57 (1993) 1470-1476
    • (1993) Bioscience Biotechnology Biochemistry , vol.57 , pp. 1470-1476
    • Lee, J.J.1    Chen, H.C.2    Jiang, S.T.3
  • 21
    • 84986465518 scopus 로고
    • Supplementation of squid fermentation with proteolytic enzymes
    • Lee Y.Z., Simpson B.K., and Haard N.F. Supplementation of squid fermentation with proteolytic enzymes. Journal of Food Biochemistry 6 (1982) 127-134
    • (1982) Journal of Food Biochemistry , vol.6 , pp. 127-134
    • Lee, Y.Z.1    Simpson, B.K.2    Haard, N.F.3
  • 22
    • 0024263314 scopus 로고
    • A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen
    • Maciewicz R.A., and Etherington D.J. A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochemistry Journal 256 (1988) 433-440
    • (1988) Biochemistry Journal , vol.256 , pp. 433-440
    • Maciewicz, R.A.1    Etherington, D.J.2
  • 23
    • 0036463587 scopus 로고    scopus 로고
    • Getting more from less - Algorithms for rapid protein identification with multiple short peptide sequences
    • Mackey A.J., Haystead T.A.J., and Pearson W.R. Getting more from less - Algorithms for rapid protein identification with multiple short peptide sequences. Molecular & Cellular Proteomics 1 2 (2002) 139-147
    • (2002) Molecular & Cellular Proteomics , vol.1 , Issue.2 , pp. 139-147
    • Mackey, A.J.1    Haystead, T.A.J.2    Pearson, W.R.3
  • 24
    • 0023627662 scopus 로고
    • Rat brain cathepsin L: Characterization and differentiation from cathepsin B utilizing opioid peptides
    • Marks N., and Berg M.J. Rat brain cathepsin L: Characterization and differentiation from cathepsin B utilizing opioid peptides. Archives Biochemistry Biophysics 259 (1987) 131-143
    • (1987) Archives Biochemistry Biophysics , vol.259 , pp. 131-143
    • Marks, N.1    Berg, M.J.2
  • 27
    • 0018940824 scopus 로고
    • Purification and some properties of a myofibrillar protein-degrading protease, cathepsin L, from rabbit skeletal muscle
    • Okitani A., Matsumura U., Kato H., and Fujimaki M. Purification and some properties of a myofibrillar protein-degrading protease, cathepsin L, from rabbit skeletal muscle. Journal of Biochemistry 87 (1980) 1133-1143
    • (1980) Journal of Biochemistry , vol.87 , pp. 1133-1143
    • Okitani, A.1    Matsumura, U.2    Kato, H.3    Fujimaki, M.4
  • 28
    • 0002849637 scopus 로고
    • Comparative action of cathepsins D, B, H, L and of a new lysosomal proteinase on rabbit myofibrils
    • Ouali A., Garrel A., Obled A., Deval C., Valin C., and Penny I. Comparative action of cathepsins D, B, H, L and of a new lysosomal proteinase on rabbit myofibrils. Meat Science 19 (1987) 83-100
    • (1987) Meat Science , vol.19 , pp. 83-100
    • Ouali, A.1    Garrel, A.2    Obled, A.3    Deval, C.4    Valin, C.5    Penny, I.6
  • 29
    • 0009827188 scopus 로고
    • Proteolytic and peptidasic activities of a particulate fraction of Loligo vulgaris Lamarck hepatopancreas
    • Pignero A., and Rocca E. Proteolytic and peptidasic activities of a particulate fraction of Loligo vulgaris Lamarck hepatopancreas. Comparative Biochemistry & Physiology 29 (1969) 1271-1275
    • (1969) Comparative Biochemistry & Physiology , vol.29 , pp. 1271-1275
    • Pignero, A.1    Rocca, E.2
  • 31
    • 0030355661 scopus 로고    scopus 로고
    • Comparison of cathepsin B, D, H and L activity in four species of Pacific fish
    • Porter R., Koury B., and Stone F. Comparison of cathepsin B, D, H and L activity in four species of Pacific fish. Journal of Food Biochemistry 19 6 (1996) 429-442
    • (1996) Journal of Food Biochemistry , vol.19 , Issue.6 , pp. 429-442
    • Porter, R.1    Koury, B.2    Stone, F.3
  • 33
    • 84872888446 scopus 로고    scopus 로고
    • Raksakulthai, R. (2001). Purification and characterization of exopeptidases from Atlantic short finned squid (Illex illecebrosus) and their application to Cheddar cheese ripening. FST (p. 241). Davis, CA: University of California, Davis.
    • Raksakulthai, R. (2001). Purification and characterization of exopeptidases from Atlantic short finned squid (Illex illecebrosus) and their application to Cheddar cheese ripening. FST (p. 241). Davis, CA: University of California, Davis.
  • 34
    • 0033243862 scopus 로고    scopus 로고
    • Purification and characterization of aminopeptidase fractions from squid (Illex illecebrosus) hepatopancreas
    • Raksakulthai R., and Haard N.F. Purification and characterization of aminopeptidase fractions from squid (Illex illecebrosus) hepatopancreas. Journal of Food Biochemistry 23 2 (1999) 123-144
    • (1999) Journal of Food Biochemistry , vol.23 , Issue.2 , pp. 123-144
    • Raksakulthai, R.1    Haard, N.F.2
  • 35
    • 0034774884 scopus 로고    scopus 로고
    • Purification and characterization of a carboxypeptidase from squid hepatopancreas (Illex illecebrosus)
    • Raksakulthai R., and Haard N.F. Purification and characterization of a carboxypeptidase from squid hepatopancreas (Illex illecebrosus). Journal of Agricultural and Food Chemistry 49 10 (2001) 5019-5030
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.10 , pp. 5019-5030
    • Raksakulthai, R.1    Haard, N.F.2
  • 37
    • 0022219885 scopus 로고
    • Rat mammary gland in culture secretes a stable high molecular weight form of cathepsin L
    • Recklies A.D., and Mort J.S. Rat mammary gland in culture secretes a stable high molecular weight form of cathepsin L. Biochemical and Biophysical Research Communications 131 (1985) 402-407
    • (1985) Biochemical and Biophysical Research Communications , vol.131 , pp. 402-407
    • Recklies, A.D.1    Mort, J.S.2
  • 38
    • 0026683629 scopus 로고
    • Purification and characterization of a collagenolytic property of renal cathepsin L from arthritic rat
    • Reddy C.K., and Dhar S.C. Purification and characterization of a collagenolytic property of renal cathepsin L from arthritic rat. International Journal of Biochemistry 24 (1992) 1465-1473
    • (1992) International Journal of Biochemistry , vol.24 , pp. 1465-1473
    • Reddy, C.K.1    Dhar, S.C.2
  • 40
    • 30944444115 scopus 로고    scopus 로고
    • An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L
    • Sasaki S.D., Cotrin S.S., Carmona A.K., and Tanaka A.S. An unexpected inhibitory activity of Kunitz-type serine proteinase inhibitor derived from Boophilus microplus trypsin inhibitor on cathepsin L. Biochemical and Biophysical Research Communications 341 1 (2006) 266-272
    • (2006) Biochemical and Biophysical Research Communications , vol.341 , Issue.1 , pp. 266-272
    • Sasaki, S.D.1    Cotrin, S.S.2    Carmona, A.K.3    Tanaka, A.S.4
  • 43
    • 0025959153 scopus 로고
    • Photometric or fluorometric assay of cathepsin-B, cathepsin-L and cathepsin-H and papain using substrates with an aminotrifluoromethylcoumarin leaving group
    • Tchoupe J.R., Moreau T., Gauthier F., and Bieth J.G. Photometric or fluorometric assay of cathepsin-B, cathepsin-L and cathepsin-H and papain using substrates with an aminotrifluoromethylcoumarin leaving group. Biochimica Et Biophysica Acta 1076 1 (1991) 149-151
    • (1991) Biochimica Et Biophysica Acta , vol.1076 , Issue.1 , pp. 149-151
    • Tchoupe, J.R.1    Moreau, T.2    Gauthier, F.3    Bieth, J.G.4
  • 44
    • 0029882882 scopus 로고    scopus 로고
    • Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide
    • Volkel H., Kurtz U., Linder J., Klumpp S., Gnau V., Jung G., et al. Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide. European Journal of Biochemistry 238 (1996) 198-206
    • (1996) European Journal of Biochemistry , vol.238 , pp. 198-206
    • Volkel, H.1    Kurtz, U.2    Linder, J.3    Klumpp, S.4    Gnau, V.5    Jung, G.6
  • 46
    • 77957100662 scopus 로고
    • In gel digestion of SDS PAGE-separated proteins: Observations from internal sequencing of 25 proteins
    • Crabb J.W. (Ed), Academic Press, San Diego, CA
    • Williams K.R., and Stone K.L. In gel digestion of SDS PAGE-separated proteins: Observations from internal sequencing of 25 proteins. In: Crabb J.W. (Ed). Techniques in protein chemistry VI (1995), Academic Press, San Diego, CA 143-152
    • (1995) Techniques in protein chemistry VI , pp. 143-152
    • Williams, K.R.1    Stone, K.L.2
  • 47
    • 0025368356 scopus 로고
    • Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta
    • Yamashita M., and Konagaya S. Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta. Comparative Biochemistry & Physiology, B 96 (1990) 247-252
    • (1990) Comparative Biochemistry & Physiology, B , vol.96 , pp. 247-252
    • Yamashita, M.1    Konagaya, S.2


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