메뉴 건너뛰기




Volumn 53, Issue 20, 2005, Pages 7667-7672

Purification and identification of a protease inhibitor from glassfish (Liparis tanakai) eggs

Author keywords

Cysteine protease; Glassfish egg; Inhibitor constant; Protease inhibitor; Stability

Indexed keywords

CATHEPSIN; PROTEINASE INHIBITOR;

EID: 27144551320     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0482459     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 0030268358 scopus 로고    scopus 로고
    • Roles endogenous enzymes in surimi gelation
    • An, H.; Peters, M. Y.; Seymour, T. A. Roles endogenous enzymes in surimi gelation. J. Food. Sci. 1996, 7, 321-327.
    • (1996) J. Food. Sci. , vol.7 , pp. 321-327
    • An, H.1    Peters, M.Y.2    Seymour, T.A.3
  • 2
    • 0029143453 scopus 로고
    • Purification and characterization of a multicatalytic proteinase from Atlantic salmon (Salmo salar) muscle
    • Stoknes, I.; Rustad, T. Purification and characterization of a multicatalytic proteinase from Atlantic salmon (Salmo salar) muscle. Comp. Biochem. Physiol. 1995, 111B(4), 587-596.
    • (1995) Comp. Biochem. Physiol. , vol.111 B , Issue.4 , pp. 587-596
    • Stoknes, I.1    Rustad, T.2
  • 3
    • 0037334270 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin L in arrowtooth flounder (Atheresthes stomias) muscle
    • Visessanguan, W.; Benjakul, S. An, H. Purification and characterization of cathepsin L in arrowtooth flounder (Atheresthes stomias) muscle. Comput. Biochem. Physiol. 2003, 134, 477-487.
    • (2003) Comput. Biochem. Physiol. , vol.134 , pp. 477-487
    • Visessanguan, W.1    Benjakul, S.2    An, H.3
  • 4
    • 0025368356 scopus 로고
    • Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta
    • Yamashita, M.; Konagaya, S. Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol. 1990, 96B, 247-252.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 247-252
    • Yamashita, M.1    Konagaya, S.2
  • 5
    • 84987350929 scopus 로고
    • Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white
    • Hamman, D. D.; Amato, P. M.; Wu, M. C.; Foegeding, E. A. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J. Food. Sci. 1990, 55 (3), 665-669.
    • (1990) J. Food. Sci. , vol.55 , Issue.3 , pp. 665-669
    • Hamman, D.D.1    Amato, P.M.2    Wu, M.C.3    Foegeding, E.A.4
  • 6
    • 84919617127 scopus 로고
    • Cathepsin degradation of Pacific whiting surimi proteins
    • An, H. Weerasinghe, V.; Seymour, T. S.; Morrissey, M. T. Cathepsin degradation of Pacific whiting surimi proteins. J. Food. Sci. 1994, 59 (5), 1013-1017.
    • (1994) J. Food. Sci. , vol.59 , Issue.5 , pp. 1013-1017
    • An, H.1    Weerasinghe, V.2    Seymour, T.S.3    Morrissey, M.T.4
  • 7
    • 0003091433 scopus 로고
    • Proteolysis in Pacific Whiting and Effect of Surimi Processing
    • Morrissey, M. T.; Hartley, P. S.; An, H. Proteolysis in Pacific Whiting and Effect of Surimi Processing. J. Aqua. Food. Product. Technol. 1995, 4(4), 5-18.
    • (1995) J. Aqua. Food. Product. Technol. , vol.4 , Issue.4 , pp. 5-18
    • Morrissey, M.T.1    Hartley, P.S.2    An, H.3
  • 9
    • 0034736002 scopus 로고    scopus 로고
    • Transcriptional factor AP-2γ increase human cystatin A gene transcription of keratinocytes
    • Takahashi, H.; Oyama, N.; Itoh, Y.; Yamamoto, A. I. Transcriptional factor AP-2γ increase human cystatin A gene transcription of keratinocytes. Biochem. Biophys. Res. Commun. 2000, 278, 719-723.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 719-723
    • Takahashi, H.1    Oyama, N.2    Itoh, Y.3    Yamamoto, A.I.4
  • 10
    • 0037288536 scopus 로고    scopus 로고
    • Evolution of the cystatin B gene: Implications for the origin of its variable dodecamer tandem repeat in humans
    • Osawa, M.; Kaneko, M.; Horiuchi, H.; Kitano, T.; Kawamoto, Y.; Saiou, N.; Umetsu, K. Evolution of the cystatin B gene: Implications for the origin of its variable dodecamer tandem repeat in humans. Genomics 2003, 81, 78-84.
    • (2003) Genomics , vol.81 , pp. 78-84
    • Osawa, M.1    Kaneko, M.2    Horiuchi, H.3    Kitano, T.4    Kawamoto, Y.5    Saiou, N.6    Umetsu, K.7
  • 11
    • 0032215157 scopus 로고    scopus 로고
    • Expression of cysteine proteinases and their inhibitor, cystatin β, in cultured rat mesangial cells
    • Makita, Y.; Ishidoh, K.; Kominami, E.; Funabiki, K.; Koide, H.; Tomino, Y. Expression of cysteine proteinases and their inhibitor, cystatin β, in cultured rat mesangial cells. J. Diab. Comput. 1998, 12, 328-336.
    • (1998) J. Diab. Comput. , vol.12 , pp. 328-336
    • Makita, Y.1    Ishidoh, K.2    Kominami, E.3    Funabiki, K.4    Koide, H.5    Tomino, Y.6
  • 12
    • 12944256812 scopus 로고
    • Cystatin S and the related cysteine proteinase inhibitors in human saliva
    • Turk, V. Ed.; Walter de Gruyter: Berlin, German
    • Isemura, S.; Saitoh, E.; Sanada, K.; Isemura, M.; Ito, S. Cystatin S and the related cysteine proteinase inhibitors in human saliva. In Cystatin Proteinases and Their Inhibitors, 1st ed.; Turk, V. Ed.; Walter de Gruyter: Berlin, German, 1986; pp 497-505.
    • (1986) Cystatin Proteinases and Their Inhibitors, 1st Ed. , pp. 497-505
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3    Isemura, M.4    Ito, S.5
  • 13
    • 0024971526 scopus 로고
    • Chicken egg white cystatin. Molecular cloning, nucleotide sequencing, and tissue distribution
    • Colella, R.; Sakaguchi, Y.; Nagase, H.; Bird, J. W. Chicken egg white cystatin. Molecular cloning, nucleotide sequencing, and tissue distribution. J. Biol. Chem. 1989, 264, 17164-17169.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17164-17169
    • Colella, R.1    Sakaguchi, Y.2    Nagase, H.3    Bird, J.W.4
  • 14
    • 0034900394 scopus 로고    scopus 로고
    • Comparison in localization between cystatin C and cathepsin K in osteoclasts and other cells in mouse tibia epiphysis by immunolight and immunoelectron microscopy
    • Yamaza, T.; Tsuji, Y.; Goto, T.; Kaido, M. A.; Nishijima, K.; Moroi, R.; Akamine, A.; Tanaka, T. Comparison in localization between cystatin C and cathepsin K in osteoclasts and other cells in mouse tibia epiphysis by immunolight and immunoelectron microscopy. Bone 2001, 29 (1), 42-53.
    • (2001) Bone , vol.29 , Issue.1 , pp. 42-53
    • Yamaza, T.1    Tsuji, Y.2    Goto, T.3    Kaido, M.A.4    Nishijima, K.5    Moroi, R.6    Akamine, A.7    Tanaka, T.8
  • 15
    • 0028147305 scopus 로고
    • Monoclonal antibodies as probes to detect conformational changes in the rat cysteine proteinase inhibitor cystatin A
    • Takeda, A.; Iwasawa, A.; Nakamura, Y.; Omata, K.; Nakaya, K. Monoclonal antibodies as probes to detect conformational changes in the rat cysteine proteinase inhibitor cystatin A. J. Immunol. Methods. 1994, 168, 69-78.
    • (1994) J. Immunol. Methods , vol.168 , pp. 69-78
    • Takeda, A.1    Iwasawa, A.2    Nakamura, Y.3    Omata, K.4    Nakaya, K.5
  • 16
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin)
    • Abe, K.; Emori, Y.; Kondo, H.; Suzuki, K.; Arai, S. Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). J. Biol. Chem. 1987, 262, 16793-16797.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 17
    • 0002486962 scopus 로고
    • Cysteine protease inhibitors of the cystatin superfamily
    • Barrett, A. J., Salvesen, D., Eds.; Elsevier: Amsterdam, Holland
    • Barrett, A. J.; Rawlings, N. D.; Davies, M. E.; Macleidt, W.; Salvesen, G.; Turk, V. Cysteine protease inhibitors of the cystatin superfamily. In Proteinase Inhibitors; Barrett, A. J., Salvesen, D., Eds.; Elsevier: Amsterdam, Holland, 1986; pp 515-569.
    • (1986) Proteinase Inhibitors , pp. 515-569
    • Barrett, A.J.1    Rawlings, N.D.2    Davies, M.E.3    Macleidt, W.4    Salvesen, G.5    Turk, V.6
  • 19
    • 0025787834 scopus 로고
    • Cysteine protease inhibitor in egg of chum salmon
    • Yamashita, M.; Konagaya, S. Cysteine protease inhibitor in egg of chum salmon. J. Biochem. 1991, 110, 762-766.
    • (1991) J. Biochem. , vol.110 , pp. 762-766
    • Yamashita, M.1    Konagaya, S.2
  • 20
    • 0141990756 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.; Kalkkinen, N.; Paulin, L. A new type of cysteine proteinase inhibitor-the salrin gene from Atlantic salmon (Salmo salar L) and Arctic charr (Salvelinus alpinus). Biochemistry 2003, 01, 001-005.
    • (2003) Biochemistry , vol.1 , pp. 1-5
    • Olenen, A.1    Kalkkinen, N.2    Paulin, L.3
  • 22
    • 0021770918 scopus 로고
    • Similarity in gene organization and homology between proteins of animal picorviruses and a plant comovirus suggest common ancestry of these virus families
    • Argos, P.; Kamer, G.; Nicklin, M. J. H.; Wimmer, E. Similarity in gene organization and homology between proteins of animal picorviruses and a plant comovirus suggest common ancestry of these virus families. Nucleic Acid Res. 1984, 12, 7251-7267.
    • (1984) Nucleic Acid Res. , vol.12 , pp. 7251-7267
    • Argos, P.1    Kamer, G.2    Nicklin, M.J.H.3    Wimmer, E.4
  • 23
    • 0031890686 scopus 로고    scopus 로고
    • Protease I inhibitor system in fish muscle: A comparative study
    • Borla, O. O.; Martone, C. B.; Sanchez, J. J. Protease I inhibitor system in fish muscle: A comparative study. Comp. Biochem. Physiol. 1998, 119B (1), 101-105.
    • (1998) Comp. Biochem. Physiol. , vol.119 B , Issue.1 , pp. 101-105
    • Borla, O.O.1    Martone, C.B.2    Sanchez, J.J.3
  • 24
    • 0000870544 scopus 로고
    • Die Kinetik der invertinwerkung
    • Michaelis, L.; Menten, M. L. Die Kinetik der invertinwerkung. Biochem. Z. 1913, 49, 333-369.
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 25
    • 0004262303 scopus 로고
    • Logman Group Ltd.: London
    • Dixon, M. Webb, E. C. Enzymes; Logman Group Ltd.: London, 1979; p 556.
    • (1979) Enzymes , pp. 556
    • Dixon, M.1    Webb, E.C.2
  • 26
    • 84911229134 scopus 로고
    • Cleavage of structure protein during the assembly of the head bacteriophage
    • Laemmli, U. K. Cleavage of structure protein during the assembly of the head bacteriophage. Nature 1970, 227, 265-275.
    • (1970) Nature , vol.227 , pp. 265-275
    • Laemmli, U.K.1
  • 27
    • 27144537653 scopus 로고    scopus 로고
    • Protein blotting by the semidry method
    • Walker, J. M., Eds.; Humana Press: Totowa, NJ
    • Gravel, P. Protein blotting by the semidry method. In The Protein Protocols Handbook; Walker, J. M., Eds.; Humana Press: Totowa, NJ, 2002; pp 321-334.
    • (2002) The Protein Protocols Handbook , pp. 321-334
    • Gravel, P.1
  • 28
    • 77957034551 scopus 로고
    • Cystatin, the egg white inhibitor of cysteine proteinases
    • Barrett, A. J. Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymol. 1981, 80, 771-778.
    • (1981) Methods Enzymol. , vol.80 , pp. 771-778
    • Barrett, A.J.1
  • 29
    • 0009070296 scopus 로고
    • Size-exclusion HPLC of protein
    • Oliver, R. W. A., Ed.; Oxford University Press: Oxford
    • Welling, G. W.; Wester, S. W. Size-exclusion HPLC of protein. In HPLC Macromolecules. A Practical Approach, 2nd ed.; Oliver, R. W. A., Ed.; Oxford University Press: Oxford, 1989; pp 77-89.
    • (1989) HPLC Macromolecules. A Practical Approach, 2nd Ed. , pp. 77-89
    • Welling, G.W.1    Wester, S.W.2
  • 30
    • 0023229953 scopus 로고
    • Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C
    • Abrahamson, M.; Grubb, A.; Olafsson, I.; Lundwall, A. Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett. 1987, 216 (2), 229-233.
    • (1987) FEBS Lett. , vol.216 , Issue.2 , pp. 229-233
    • Abrahamson, M.1    Grubb, A.2    Olafsson, I.3    Lundwall, A.4
  • 31
    • 0025817602 scopus 로고
    • Minireview, The cystatins: Protein inhibitors of cysteine proteinase
    • Turk, V.; Bode, W. Minireview, The cystatins: Protein inhibitors of cysteine proteinase. Fed. Eur. Biochem. Soc. 1991, 285 (2), 213-219.
    • (1991) Fed. Eur. Biochem. Soc. , vol.285 , Issue.2 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 32
    • 0033834190 scopus 로고    scopus 로고
    • Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants
    • Wu, J.; Haard, N. F. Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants. Comp. Biochem. Physiol. 2000, 127, 209-220.
    • (2000) Comp. Biochem. Physiol. , vol.127 , pp. 209-220
    • Wu, J.1    Haard, N.F.2
  • 33
    • 0003179675 scopus 로고
    • The expression of papain inhibitor during development of cowpea seeds
    • Fernandes, K. V. S.; Campos, F. A. P.; Do-Val, R. R.; Xavier-Filho, J. The expression of papain inhibitor during development of cowpea seeds. Plant Sci. 1991, 74, 179-184.
    • (1991) Plant Sci. , vol.74 , pp. 179-184
    • Fernandes, K.V.S.1    Campos, F.A.P.2    Do-Val, R.R.3    Xavier-Filho, J.4
  • 34
    • 0032476613 scopus 로고    scopus 로고
    • Leaves of transgenic tomato plants overexpressing prosystemin accumulate high levels of cystatin
    • Jacinto, T.; Fernandes, K. V. S.; Machado, O. L. T.; Siqueira, C. L., Jr. Leaves of transgenic tomato plants overexpressing prosystemin accumulate high levels of cystatin. Plant Sci. 1998, 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
  • 35
    • 0036237099 scopus 로고    scopus 로고
    • Differential stabilities of alkaline protease inhibitor from Actinomycetes: Effect of various additives on thermostability
    • Pandhare, J.; Zog, K.; Deshpande, V. V. Differential stabilities of alkaline protease inhibitor from Actinomycetes: Effect of various additives on thermostability. Biores. Technol. 2002, 84 165-169.
    • (2002) Biores. Technol. , vol.84 , pp. 165-169
    • Pandhare, J.1    Zog, K.2    Deshpande, V.V.3
  • 36
    • 21144465354 scopus 로고
    • Cathepsin L-like protease in Pacific hake muscle infected by myxosporidian parasites
    • Toyohara, H.; Kinoshita, M.; Kimura, I.; Satake, M.; Sakaguchi, M. Cathepsin L-like protease in Pacific hake muscle infected by myxosporidian parasites. Nippon Suisan Gakkaishi 1993, 59, 1101-1107.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 1101-1107
    • Toyohara, H.1    Kinoshita, M.2    Kimura, I.3    Satake, M.4    Sakaguchi, M.5
  • 37
    • 0025076125 scopus 로고
    • Purification and characterization of cathepsin B from white muscle of chum salmon, Oncorhynchus keta
    • Yamashita, M.; Konagaya, S. Purification and characterization of cathepsin B from white muscle of chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol. 1990, 96B, 733-737.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 733-737
    • Yamashita, M.1    Konagaya, S.2
  • 38
    • 0026458505 scopus 로고
    • Differentiation and localization of catheptic proteinases responsible for extensive autolysis of mature chum salmon muscle (Oncorhynchus keta)
    • Yamashita, M.; Konagaya, S. Differentiation and localization of catheptic proteinases responsible for extensive autolysis of mature chum salmon muscle (Oncorhynchus keta). Comp. Biochem. Physiol. 1992, 103B, 483-487.
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 483-487
    • Yamashita, M.1    Konagaya, S.2
  • 39
    • 12244249166 scopus 로고    scopus 로고
    • Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle
    • Soottawat, B.; Wonnop, V.; Kittima, L. Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle. Comp. Biochem. Physiol. 2003, 134B, 579-591.
    • (2003) Comp. Biochem. Physiol. , vol.134 B , pp. 579-591
    • Soottawat, B.1    Wonnop, V.2    Kittima, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.