메뉴 건너뛰기




Volumn 16, Issue 4, 2006, Pages 524-530

Purification, characterization, and inhibitory activity of glassfish (Liparis tanakai) egg high molecular weight protease inhibitor against papain and cathepsin

Author keywords

Glassfish egg; HMW protease inhibitor; Ki; Kininogen

Indexed keywords

CATHEPSIN; CYSTEINE PROTEINASE; KININOGEN; PAPAIN; PROTEINASE INHIBITOR;

EID: 33646575897     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (47)
  • 1
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites for the cysteine protease inhibitor human cystatin C and chicken cystatin
    • Abrahamson, M., A. Ritonja, M. A. Brown, A. Grubb, W. Machleidt, and A. J. Barrett. 1987. Identification of the probable inhibitory reactive sites for the cysteine protease inhibitor human cystatin C and chicken cystatin. J. Biol. Chem. 262: 9688-9694.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3    Grubb, A.4    Machleidt, W.5    Barrett, A.J.6
  • 2
    • 0030268358 scopus 로고    scopus 로고
    • Roles of endogenous enzymes in surimi gelation
    • An, H., M. Y. Peters, and T. A. Seymour. 1996. Roles of endogenous enzymes in surimi gelation. J. Food Sci. 7: 321-326.
    • (1996) J. Food Sci. , vol.7 , pp. 321-326
    • An, H.1    Peters, M.Y.2    Seymour, T.A.3
  • 3
    • 0002486962 scopus 로고
    • Cysteine protease inhibitors of the cystatin superfamily
    • A. J. Barrett and D. Salvesen (eds.), Elsevier, Amesterdam
    • Barret, A. J., N. D. Rawlings, M. E. Davies, W. Macleidt, G. Salvesen, and V. Turk. 1986. Cysteine protease inhibitors of the cystatin superfamily, pp. 515-569. In A. J. Barrett and D. Salvesen (eds.), Proteinase Inhibitors. Elsevier, Amesterdam.
    • (1986) Proteinase Inhibitors , pp. 515-569
    • Barret, A.J.1    Rawlings, N.D.2    Davies, M.E.3    Macleidt, W.4    Salvesen, G.5    Turk, V.6
  • 4
    • 0019765848 scopus 로고
    • Cathepsin B, Cathepsin H. and Cathepsin L
    • A. J. Barrett (ed.), Academic Press, San Diego, LA, U.S.A
    • Barrett, A. J. and H. Kirschke. 1981. Cathepsin B, Cathepsin H. and Cathepsin L, pp. 535-561. In A. J. Barrett (ed.), Methodes in Enzymology, vol. 80. Academic Press, San Diego, LA, U.S.A.
    • (1981) Methodes in Enzymology , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 5
    • 0031890686 scopus 로고    scopus 로고
    • Protease I inhibitor system in fish muscle: A comparative study
    • Borla, O. O., C. B. Martone, and J. J. Sánchez. 1998. Protease I inhibitor system in fish muscle: A comparative study. Comp. Biochem. Physiol. B 119: 101-105.
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 101-105
    • Borla, O.O.1    Martone, C.B.2    Sánchez, J.J.3
  • 6
    • 0032055137 scopus 로고    scopus 로고
    • Purification and characterization of a new cystatin from Taiwan cobra (Naja naja atra) venom
    • Brillard-Bourdet, M., V. Nguyen, M. Ferrer-Di Martino, F. Gauthierand, and T. Moreau. 1998. Purification and characterization of a new cystatin from Taiwan cobra (Naja naja atra) venom. Biochem. J. 331: 239-244.
    • (1998) Biochem. J. , vol.331 , pp. 239-244
    • Brillard-Bourdet, M.1    Nguyen, V.2    Ferrer-Di Martino, M.3    Gauthierand, F.4    Moreau, T.5
  • 7
    • 0027452522 scopus 로고
    • Purification of a vasoactive peptide related to lysyl-bradykinin from trout plasma
    • Conlon, J. M. and K. R. Olson. 1993. Purification of a vasoactive peptide related to lysyl-bradykinin from trout plasma. FEBS Lett. 334: 75-78.
    • (1993) FEBS Lett. , vol.334 , pp. 75-78
    • Conlon, J.M.1    Olson, K.R.2
  • 8
    • 0029079036 scopus 로고
    • Isolation and biological activity of [Trp5]bradykinin from the plasma of the phylogenetically ancient fish, the bowfin and the longnosed gar
    • Conlon, J. M., B. Platzack, L. E. Marra, J. H. Youson, and K. R. Olson. 1995. Isolation and biological activity of [Trp5]bradykinin from the plasma of the phylogenetically ancient fish, the bowfin and the longnosed gar. Peptides 16: 485-489.
    • (1995) Peptides , vol.16 , pp. 485-489
    • Conlon, J.M.1    Platzack, B.2    Marra, L.E.3    Youson, J.H.4    Olson, K.R.5
  • 9
    • 0004262303 scopus 로고
    • Logman Group Ltd., London, U.K
    • Dixon, M. and E. C. Webb. 1979. Enzymes. Logman Group Ltd., London, U.K.
    • (1979) Enzymes
    • Dixon, M.1    Webb, E.C.2
  • 11
    • 84987350929 scopus 로고
    • Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white
    • Hammann, D. D., P. M. Amato, M. C. Wu, and E. A. Foegeding. 1990. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J. Food Sci. 55: 665-669.
    • (1990) J. Food Sci. , vol.55 , pp. 665-669
    • Hammann, D.D.1    Amato, P.M.2    Wu, M.C.3    Foegeding, E.A.4
  • 13
    • 0036679896 scopus 로고    scopus 로고
    • Recent advance in the synthesis, design and selection of cysteine protease inhibitors
    • Hernandez, A. A. and W. R. Roush. 2002. Recent advance in the synthesis, design and selection of cysteine protease inhibitors. Curr. Opin. Chem. Biol. 6: 459-465.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 459-465
    • Hernandez, A.A.1    Roush, W.R.2
  • 14
    • 0032476613 scopus 로고    scopus 로고
    • Leaves of transgenic tomato plants overexpressing prosystemin accumalate high levels of cystatin
    • Jacinto, T., K. V. S. Fernandes, O. L. T. Machado, and C. L. Siqueira Jr. 1998. Leaves of transgenic tomato plants overexpressing prosystemin accumalate high levels of cystatin Plant Sci. 138: 35-42.
    • (1998) Plant Sci. , vol.138 , pp. 35-42
    • Jacinto, T.1    Fernandes, K.V.S.2    Machado, O.L.T.3    Siqueira Jr., C.L.4
  • 15
    • 33751158499 scopus 로고
    • Purification and characterization of cathepsin B from ordinary muscle of mackerel (Scomber australasicus)
    • Jiang, K., J. Lee, and H. Chen. 1994. Purification and characterization of cathepsin B from ordinary muscle of mackerel (Scomber australasicus). J. Agric. Food Chem. 42: 1073-1079.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1073-1079
    • Jiang, K.1    Lee, J.2    Chen, H.3
  • 16
    • 0030968742 scopus 로고    scopus 로고
    • Mackerel cathepsin B and L effect on thermal degradation of surimi
    • Jiang, S. T., J. J. Lee, and C. Y. Tsao. 1997. Mackerel cathepsin B and L effect on thermal degradation of surimi. J. Food Sci. 62: 1-6.
    • (1997) J. Food Sci. , vol.62 , pp. 1-6
    • Jiang, S.T.1    Lee, J.J.2    Tsao, C.Y.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophagety
    • Laemmli, U. K. 1970. Cleavage of structural protein during the assembly of the head of bacteriophagety. Nature 227: 265-275.
    • (1970) Nature , vol.227 , pp. 265-275
    • Laemmli, U.K.1
  • 18
    • 0001554239 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • J. W. Park (ed.), Marcel Dekker Inc., New York, NY, U.S.A
    • Lanier, T. C. 2000. Surimi gelation chemistry, pp. 237-266. In J. W. Park (ed.), Surimi and Surimi Seafood. Marcel Dekker Inc., New York, NY, U.S.A.
    • (2000) Surimi and Surimi Seafood , pp. 237-266
    • Lanier, T.C.1
  • 19
    • 8644287569 scopus 로고    scopus 로고
    • Purification and properties of an extracellular acid phytase from Pseudomonas fragi Y9451
    • In, M.-J., E.-S. Jang, Y.-J. Kim, and N.-S. Oh. 2004. Purification and properties of an extracellular acid phytase from Pseudomonas fragi Y9451. J. Microbiol. Biotechnol. 14: 1004-1008.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 1004-1008
    • In, M.-J.1    Jang, E.-S.2    Kim, Y.-J.3    Oh, N.-S.4
  • 21
    • 0032189176 scopus 로고    scopus 로고
    • Characterization of bradykinin-related peptides generated in the plasma of six sarcopterygian species (African lungfish, amphiuma, coachwhip, bullsnake, gila monster, and Gray's monitor)
    • Li, Z., S. M. Secor, V. A. Lance, M. A. Masini, M. Vallarino, and J. M. Conlon. 1998. Characterization of bradykinin-related peptides generated in the plasma of six sarcopterygian species (African lungfish, amphiuma, coachwhip, bullsnake, gila monster, and Gray's monitor). Gen. Comp. Endocrinol. 112: 108-114.
    • (1998) Gen. Comp. Endocrinol. , vol.112 , pp. 108-114
    • Li, Z.1    Secor, S.M.2    Lance, V.A.3    Masini, M.A.4    Vallarino, M.5    Conlon, J.M.6
  • 22
    • 0000870544 scopus 로고
    • Die Kinetik der invertinwerkung
    • Michaelis, L. and M. L. Menten. 1913. Die Kinetik der invertinwerkung. Biochem. Z. 49: 333-369.
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 23
    • 27144532005 scopus 로고    scopus 로고
    • A new type of cysteine proteinase inhibitor - The salrin gene from Atlantic salmon (Salmo salar L) and Arctic charr (Salvelinus alpinus)
    • Olenen, A., N. Kalkkinen, and L. Paulin. 2003. A new type of cysteine proteinase inhibitor - the salrin gene from Atlantic salmon (Salmo salar L) and Arctic charr (Salvelinus alpinus). Biochemie 1: 001-005.
    • (2003) Biochemie , vol.1 , pp. 001-005
    • Olenen, A.1    Kalkkinen, N.2    Paulin, L.3
  • 24
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H. H. and T. Schirmeister. 1997. Cysteine proteases and their inhibitors. Chem. Rev. 97: 133-171.
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Otto, H.H.1    Schirmeister, T.2
  • 25
    • 0030969424 scopus 로고    scopus 로고
    • Purification, structural characterization, and cardiovascular activity of cod bradykinins
    • Platzack, B. and J. M. Conlon. 1997. Purification, structural characterization, and cardiovascular activity of cod bradykinins. Am. J. Physiol. 272: R710-R717.
    • (1997) Am. J. Physiol. , vol.272
    • Platzack, B.1    Conlon, J.M.2
  • 26
    • 27944440976 scopus 로고    scopus 로고
    • An antifungal antibiotic purified from Bacillus megaterium KL39, a biocontrol agent of red-pepper Phytophthora-blight disease
    • Jung, H. K. and S.-D. Kim. 2005. An antifungal antibiotic purified from Bacillus megaterium KL39, a biocontrol agent of red-pepper Phytophthora-blight disease. J. Microbiol. Biotechnol. 15: 1001-1010.
    • (2005) J. Microbiol. Biotechnol. , vol.15 , pp. 1001-1010
    • Jung, H.K.1    Kim, S.-D.2
  • 27
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine protease inhibitor cystatin B from human liver
    • Ritonja, A., W. Machleidt, and A. J. Barrett. 1985. Amino acid sequence of the intracellular cysteine protease inhibitor cystatin B from human liver. Biochem. Biophys. Res. Commun. 131: 1187-1192.
    • (1985) Biochem. Biophys. Res. Commun. , vol.131 , pp. 1187-1192
    • Ritonja, A.1    Machleidt, W.2    Barrett, A.J.3
  • 28
    • 0030037915 scopus 로고    scopus 로고
    • The amino acid sequence, structure comparisons and inhibition kinetics of cathepsin L and sheep stefin B
    • Ritonja, A., T. H. Coetzer, R. N. Pike, and C. Dennison. 1996. The amino acid sequence, structure comparisons and inhibition kinetics of cathepsin L and sheep stefin B. Comp. Biochem. Physiol. B Biochem. B. 114: 193-198.
    • (1996) Comp. Biochem. Physiol. B Biochem. B. , vol.114 , pp. 193-198
    • Ritonja, A.1    Coetzer, T.H.2    Pike, R.N.3    Dennison, C.4
  • 29
    • 0035005375 scopus 로고    scopus 로고
    • Purification and characterization of a protease inhibitor from white croaker skeletal muscle (Micropogon opercularis)
    • Sangorrin, M. P., E. J. Folco, C. M. Martone, and J. J. Sánchez. 2001. Purification and characterization of a protease inhibitor from white croaker skeletal muscle (Micropogon opercularis). Int. J. Biochem. Cell Biol. 33: 691-699.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 691-699
    • Sangorrin, M.P.1    Folco, E.J.2    Martone, C.M.3    Sánchez, J.J.4
  • 30
    • 0015857449 scopus 로고
    • Some properties of a ficin-papain inhibitor from avian egg white
    • Sen, L. J. and J. R. Whiteker. 1973. Some properties of a ficin-papain inhibitor from avian egg white. Arch. Biochem. Biophys. 158: 623-632.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 623-632
    • Sen, L.J.1    Whiteker, J.R.2
  • 31
    • 0000219548 scopus 로고
    • Purification and characterization of cathepsin B from skeletal muscle of fresh water fish, Tilapia mossambica
    • Sharekar, S. V., M. S. Gore, and V. Ninjoor. 1988. Purification and characterization of cathepsin B from skeletal muscle of fresh water fish, Tilapia mossambica. J. Food Sci. 53: 1018-1023.
    • (1988) J. Food Sci. , vol.53 , pp. 1018-1023
    • Sharekar, S.V.1    Gore, M.S.2    Ninjoor, V.3
  • 32
    • 0022002505 scopus 로고
    • A new function of kininogens as thiol-proteinase inhibitor: Inhibition of papain and cathepsins B, H, and L by bovine, rat and human plasma kininogen
    • Sueyoshi, T., K. Enjyoji, T. Shimada, H. Kato, S. Iwanaga, Y. Bando, E. Kominami, and N. Katunuma. 1985. A new function of kininogens as thiol-proteinase inhibitor: Inhibition of papain and cathepsins B, H, and L by bovine, rat and human plasma kininogen. FEBS 182: 193-195.
    • (1985) FEBS , vol.182 , pp. 193-195
    • Sueyoshi, T.1    Enjyoji, K.2    Shimada, T.3    Kato, H.4    Iwanaga, S.5    Bando, Y.6    Kominami, E.7    Katunuma, N.8
  • 33
    • 0031674515 scopus 로고    scopus 로고
    • Purification and characterization of two cysteine proteinase inhibitors from the skin of Atlantic salmon (Salmo salar L.)
    • Synnes, M. 1998. Purification and characterization of two cysteine proteinase inhibitors from the skin of Atlantic salmon (Salmo salar L.). Comp. Biochem. Physiol. B 121: 257-264.
    • (1998) Comp. Biochem. Physiol. B , vol.121 , pp. 257-264
    • Synnes, M.1
  • 35
    • 13144284330 scopus 로고
    • Detection of a cysteine protease inhibitor in carp muscle
    • Toyohara, H., Y. Makinodan, and S. Ikeda. 1988. Detection of a cysteine protease inhibitor in carp muscle. Nippon Suisan Gakkaishi 54: 157.
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 157
    • Toyohara, H.1    Makinodan, Y.2    Ikeda, S.3
  • 37
    • 0026888604 scopus 로고
    • Isolation and characterization of bovine stefin B
    • Turk, B., I. Kriza, and V. Turk. 1992. Isolation and characterization of bovine stefin B. Biol. Chem. Hoppe Seyler 373: 441-446.
    • (1992) Biol. Chem. Hoppe Seyler , vol.373 , pp. 441-446
    • Turk, B.1    Kriza, I.2    Turk, V.3
  • 38
    • 0030570754 scopus 로고    scopus 로고
    • High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants
    • Turk, B., V. Stoka, V. Turk, G. Johansson, J. J. Cazzulo, and I. Bjork. 1996. High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants. FEBS Lett. 391: 109-112.
    • (1996) FEBS Lett. , vol.391 , pp. 109-112
    • Turk, B.1    Stoka, V.2    Turk, V.3    Johansson, G.4    Cazzulo, J.J.5    Bjork, I.6
  • 39
    • 27144551320 scopus 로고    scopus 로고
    • Purification and identification of a protease inhibitor from Glassfish (Liparis tanakai) Eggs
    • Ustadi, K. Y. Kim, and S. M. Kim. 2005. Purification and identification of a protease inhibitor from Glassfish (Liparis tanakai) Eggs. J. Agric. Food Chem. 53: 7667-7672.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7667-7672
    • Ustadi, K.1    Kim, Y.2    Kim, S.M.3
  • 40
    • 67649392930 scopus 로고    scopus 로고
    • Nondenaturing polyacrylamide gel electrophoresis of protein
    • J. M. Walker (ed.), 2nd Ed. Huana Press, Totowa, NJ, U.S.A
    • Walker, J. M. 2002. Nondenaturing polyacrylamide gel electrophoresis of protein, pp. 57-60. In J. M. Walker (ed.), The Protein Protocols Handbook, 2nd Ed. Huana Press, Totowa, NJ, U.S.A.
    • (2002) The Protein Protocols Handbook , pp. 57-60
    • Walker, J.M.1
  • 41
    • 0000118723 scopus 로고    scopus 로고
    • Characterization of active components in food grade proteinase inhibitor for surimi manufacture
    • Weerasinghe V. C., M. T. Morrissey, and H. An. 1996. Characterization of active components in food grade proteinase inhibitor for surimi manufacture. J. Food Chem. 44: 2584-2590.
    • (1996) J. Food Chem. , vol.44 , pp. 2584-2590
    • Weerasinghe, V.C.1    Morrissey, M.T.2    An, H.3
  • 42
    • 1542375101 scopus 로고    scopus 로고
    • Inhibitory effect of ginseng polysaccharides on rotavirus infection
    • Bae, E.-A., J.-E. Shin, S.-H. Park, and D.-H. Kim. 2004. Inhibitory effect of ginseng polysaccharides on rotavirus infection. J. Microbiol. Biotechnol. 14: 202-204.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 202-204
    • Bae, E.-A.1    Shin, J.-E.2    Park, S.-H.3    Kim, D.-H.4
  • 43
    • 0025368356 scopus 로고
    • Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta
    • Yamashita, M. and S. Konagaya. 1990. Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol. 96B: 247-252.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 247-252
    • Yamashita, M.1    Konagaya, S.2
  • 44
    • 0025076125 scopus 로고
    • Purification and characterization of cathepsin B from the white muscle of chum salmon, Oncorhynchus keta
    • Yamashita, M. and S. Konagaya. 1990. Purification and characterization of cathepsin B from the white muscle of chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol. 96B: 733-737.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 733-737
    • Yamashita, M.1    Konagaya, S.2
  • 45
    • 0025787834 scopus 로고
    • Cysteine protease inhibitor in egg of chum salmon
    • Yamashita, M. and S. Konagaya. 1991. Cysteine protease inhibitor in egg of chum salmon. J. Biochem. 110: 762-766.
    • (1991) J. Biochem. , vol.110 , pp. 762-766
    • Yamashita, M.1    Konagaya, S.2
  • 46
    • 0026091388 scopus 로고
    • A comparison of cystatin activity in various tissues of chum salmon (Oncorhynchus keta) between feeding and spawning migrations
    • Yamashita, M. and S. Konagaya. 1991. A comparison of cystatin activity in various tissues of chum salmon (Oncorhynchus keta) between feeding and spawning migrations. Comp. Biochem. Physiol. A 100: 749-751.
    • (1991) Comp. Biochem. Physiol. A , vol.100 , pp. 749-751
    • Yamashita, M.1    Konagaya, S.2
  • 47
    • 0033572814 scopus 로고    scopus 로고
    • Atlantic salmon (Salmo salar L) skin contains a novel kininogen and another cysteine proteinase inhibitor
    • Ylonen, A., A. Rinne, J. Herttuainen, J. Bogwald, M. Jarvinen, and N. Kalkkinen. 1999. Atlantic salmon (Salmo salar L) skin contains a novel kininogen and another cysteine proteinase inhibitor. Eur. J. Biochem. 266: 1066-1072.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1066-1072
    • Ylonen, A.1    Rinne, A.2    Herttuainen, J.3    Bogwald, J.4    Jarvinen, M.5    Kalkkinen, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.