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Volumn 125, Issue 4, 2000, Pages 493-502

Rainbow trout (Oncorhynchus mykiss) cystatin C: Expression in Escherichia coli and properties of the recombinant protease inhibitor

Author keywords

Bacterial expression; Cystatin; Disulfide linkage; Protease; Protease inhibitor; Protein refolding; Salmonid; Trout

Indexed keywords

CYSTATIN C; PROTEINASE INHIBITOR;

EID: 0034007099     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(00)00156-5     Document Type: Article
Times cited : (17)

References (35)
  • 2
    • 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., 1987a. Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett. 216, 229-233.
    • (1987) FEBS Lett. , vol.216 , pp. 229-233
    • Abrahamson, M.1    Grubb, A.2    Olafsson, I.3    Lundwall, A.4
  • 3
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites for the cysteine proteinase inhibitors human cystatin C and chicken cystatin
    • Abrahamson, M., Ritonja, A., Brown, M.A., Grubb, A., Machleidt, W., Barrett, A.J., 1987b. Identification of the probable inhibitory reactive sites for the cysteine proteinase inhibitors 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
  • 4
    • 0023684074 scopus 로고
    • Efficient production of native, biologically active human cystatin C by Escherichia coli
    • Abrahamson, M., Dalboge, H., Olafsson, I., Carlsen, S., Grubb, A., 1988. Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett. 236, 14-18.
    • (1988) FEBS Lett. , vol.236 , pp. 14-18
    • Abrahamson, M.1    Dalboge, H.2    Olafsson, I.3    Carlsen, S.4    Grubb, A.5
  • 5
    • 0018722049 scopus 로고
    • Practical consideration in the design of initial velocity enzyme rate assays
    • Allison, R.D., Purich, D.L., 1979. Practical consideration in the design of initial velocity enzyme rate assays. Methods Enzymol. 63, 3-22.
    • (1979) Methods Enzymol. , vol.63 , pp. 3-22
    • Allison, R.D.1    Purich, D.L.2
  • 6
    • 0024494090 scopus 로고
    • Synthesis a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation
    • Auerswald, E.A., Genenger, G., Assfalg-Machleidt, I., Kos, J., Bode, W., 1989. Synthesis a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation. FEBS Lett. 243, 186-192.
    • (1989) FEBS Lett. , vol.243 , pp. 186-192
    • Auerswald, E.A.1    Genenger, G.2    Assfalg-Machleidt, I.3    Kos, J.4    Bode, W.5
  • 8
    • 0015338074 scopus 로고
    • A new assay for cathepsin B1 and other thiol proteinases
    • Barrett, A.J., 1972. A new assay for cathepsin B1 and other thiol proteinases. Anal. Biochem. 47, 280-293.
    • (1972) Anal. Biochem. , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 9
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A.J., Kirschre, H., 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80, 535-539.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-539
    • Barrett, A.J.1    Kirschre, H.2
  • 10
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogs as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A.J., Kembhavi, A.A., Brown, M.A., Kirschke, H., Knight, C.G., Tamai, M., Hanada, K., 1982. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogs as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 11
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Eschcrichia coli cytoplasm
    • Bessette, P.H., Aslund, F., Beckwith, J., Georgiou, G., 1999. Efficient folding of proteins with multiple disulfide bonds in the Eschcrichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96, 13703-13708.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 13
    • 0024971526 scopus 로고
    • Chicken egg white cystatin-molecular cloning, nucleotide sequence, and tissue distribution
    • Colella, R., Sakaguchi, Y., Nagase, H., Bird, J.W.C., 1989. Chicken egg white cystatin-molecular cloning, nucleotide sequence, and tissue distribution. J. Biol. Chem. 264, 17164-17169.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17164-17169
    • Colella, R.1    Sakaguchi, Y.2    Nagase, H.3    Bird, J.W.C.4
  • 14
    • 0026907372 scopus 로고
    • Fish embryo cell cultures for derivation of stem cells and transgenic chimeras
    • Collodi, P., Kamei, Y., Sharps, A., Weber, D., Barnes, D., 1992. Fish embryo cell cultures for derivation of stem cells and transgenic chimeras. Mol. Mar. Biol. Biotech. 1, 257-265.
    • (1992) Mol. Mar. Biol. Biotech. , vol.1 , pp. 257-265
    • Collodi, P.1    Kamei, Y.2    Sharps, A.3    Weber, D.4    Barnes, D.5
  • 16
    • 0027242118 scopus 로고
    • Human cystatin D: CDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva
    • Freije, J.P., Balbin, M., Abrahamson, M., Velasco, G., Dalboge, H., Grubb, A., Lopez-Otin, C., 1993. Human cystatin D: cDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva. J. Biol. Chem. 268, 15737-15744.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15737-15744
    • Freije, J.P.1    Balbin, M.2    Abrahamson, M.3    Velasco, G.4    Dalboge, H.5    Grubb, A.6    Lopez-Otin, C.7
  • 17
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • Garcia-Carreno, F.L., Dimes, L.E., Haard, N.F., 1993. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem. 214, 65-69.
    • (1993) Anal. Biochem. , vol.214 , pp. 65-69
    • Garcia-Carreno, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 19
    • 0029744913 scopus 로고    scopus 로고
    • Mouse and rat cystatin C: Escherichia coli production, characterization and tissue distribution
    • Hakansson, K., Huh, C., Grubb, A., Karlsson, S., Abrahamson, M., 1996. Mouse and rat cystatin C: Escherichia coli production, characterization and tissue distribution. Comp. Biochem. Physiol. B 114, 303-311.
    • (1996) Comp. Biochem. Physiol. B , vol.114 , pp. 303-311
    • Hakansson, K.1    Huh, C.2    Grubb, A.3    Karlsson, S.4    Abrahamson, M.5
  • 20
    • 12944256812 scopus 로고
    • Cystatin S and the related cysteine proteinase inhibitors in human saliva
    • Turk, V. (Ed.), Walter de Gruyter, Berlin
    • Isemura, S., Saitoh, E., Sanada, K., Isemura, M., Ito, S., 1986. Cystatin S and the related cysteine proteinase inhibitors in human saliva. In: Turk, V. (Ed.), Cystatin Proteinases and Their Inhibitors. Walter de Gruyter, Berlin, pp. 497-505.
    • (1986) Cystatin Proteinases and Their Inhibitors , pp. 497-505
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3    Isemura, M.4    Ito, S.5
  • 21
    • 0001821050 scopus 로고
    • Oryzacystatin and other proteinase inhibitors in rice grain: Potential use as a fish processing aid
    • Izquierdo-Pulido, M.L., Haard, T.A., Hung, J., Haard, N.F., 1994. Oryzacystatin and other proteinase inhibitors in rice grain: potential use as a fish processing aid. J. Agric. Food Chem. 42, 616-622.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 616-622
    • Izquierdo-Pulido, M.L.1    Haard, T.A.2    Hung, J.3    Haard, N.F.4
  • 22
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser, C.A., Preuss, D., Grisafi, P., Botstein, D., 1987. Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 235, 312-315.
    • (1987) Science , vol.235 , pp. 312-315
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Botstein, D.4
  • 23
    • 85007961892 scopus 로고
    • The complete amino acid sequence of pituitary cystatin from chum salmon
    • Koide, Y., Noso, T., 1994. The complete amino acid sequence of pituitary cystatin from chum salmon. Biosci. Biotech. Biochem. 58, 164-169.
    • (1994) Biosci. Biotech. Biochem. , vol.58 , pp. 164-169
    • Koide, Y.1    Noso, T.2
  • 24
    • 12944274499 scopus 로고
    • Isolation and characterization of chicken egg white low-Mr kininogen
    • Turk, V. (Ed.), Walter de Gruyter, Berlin
    • Kos, J., Dolinar, M., Turk, V., 1986. Isolation and characterization of chicken egg white low-Mr kininogen. In: Turk, V. (Ed.), Cysteine Proteinases and Their Inhibitors. Walter de Gruyter, Berlin, pp. 583-591.
    • (1986) Cysteine Proteinases and Their Inhibitors , pp. 583-591
    • Kos, J.1    Dolinar, M.2    Turk, V.3
  • 26
  • 27
    • 0026570448 scopus 로고
    • Interaction of recombinant human cystatin C with the cysteine proteinase papain and actinidin
    • Lindahl, P., Abrahamson, M., Bjork, I., 1992. Interaction of recombinant human cystatin C with the cysteine proteinase papain and actinidin. Biochem. J. 281, 49-55.
    • (1992) Biochem. J. , vol.281 , pp. 49-55
    • Lindahl, P.1    Abrahamson, M.2    Bjork, I.3
  • 28
    • 84893743812 scopus 로고
    • Effect of food grade protease inhibitors on autolysis and gel strength of surimi
    • Morrissey, M.T., Wu, J.W., Lin, D.D., An, H., 1993. Effect of food grade protease inhibitors on autolysis and gel strength of surimi. J. Food Sci. 58, 1050-1054.
    • (1993) J. Food Sci. , vol.58 , pp. 1050-1054
    • Morrissey, M.T.1    Wu, J.W.2    Lin, D.D.3    An, H.4
  • 29
    • 0021676681 scopus 로고
    • Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin
    • Nicklin, M.J.H., Barrett, A.J., 1984. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 223, 245-253.
    • (1984) Biochem. J. , vol.223 , pp. 245-253
    • Nicklin, M.J.H.1    Barrett, A.J.2
  • 31
    • 0024996689 scopus 로고
    • Transforming growth factor b regulates cystatin C in serum-free mouse embryo (SFME) cells
    • Solem, M.L., Rawson, C., Lindburg, K., Barnes, D.W., 1990. Transforming growth factor b regulates cystatin C in serum-free mouse embryo (SFME) cells. Biochem. Biophys. Res. Commun. 172, 945-951.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 945-951
    • Solem, M.L.1    Rawson, C.2    Lindburg, K.3    Barnes, D.W.4
  • 34
    • 0025787834 scopus 로고
    • Cysteine protease inhibitor in egg of chum salmon
    • Yamashita, M., Konagaya, S., 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
  • 35
    • 0029783886 scopus 로고    scopus 로고
    • Molecular cloning and gene expression of chum salmon cystatin
    • Yamashita, M., Konagaya, S., 1996. Molecular cloning and gene expression of chum salmon cystatin. J. Biochem. 120, 483-487.
    • (1996) J. Biochem. , vol.120 , pp. 483-487
    • Yamashita, M.1    Konagaya, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.