메뉴 건너뛰기




Volumn 48, Issue 6, 2000, Pages 2602-2607

Overexpression of the soluble form of chicken cystatin in Escherichia coli and its purification

Author keywords

Chicken cystatin; Cysteine proteinase inhibitor; E. coli AD494(DE3)pLysS; Overexpression; PET 23a(+)

Indexed keywords

CATHEPSIN; COMPLEMENTARY DNA; CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; MESSENGER RNA; PAPAIN; RECOMBINANT PROTEIN;

EID: 0033937731     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf000058x     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 85004645817 scopus 로고
    • Purification and characterization of a rice cysteine proteinase inhibitor
    • Abe, K.; Hiroto, K.; Arai, S. Purification and characterization of a rice cysteine proteinase inhibitor. Agric. Biol. Chem. 1987, 51, 2763-2765.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2763-2765
    • Abe, K.1    Hiroto, K.2    Arai, S.3
  • 2
    • 0024278653 scopus 로고
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of cystatin superfamily
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of cystatin superfamily. J. Biol. Chem. 1988, 236, 7655-7659.
    • (1988) J. Biol. Chem. , vol.236 , pp. 7655-7659
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Arai, S.4    Suzuki, K.5
  • 3
    • 0026497716 scopus 로고
    • Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies
    • Abe, M.; Abe, K.; Kuroda, M.; Arai, S. Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies. Eur. J. Biochem. 1992, 209, 933-937.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 933-937
    • Abe, M.1    Abe, K.2    Kuroda, M.3    Arai, S.4
  • 4
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin c and chicken cystatin
    • Abrahamson, M.; Ritonja, A.; Brown, M. A.; Grubb, A.; Machleidt, W.; Barrett, A. J. Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin c and chicken cystatin. J. Biol. Chem. 1987, 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
  • 5
    • 0025964356 scopus 로고
    • Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase
    • Abrahamson, M.; Mason, R. W.; Hansson, H.; Buttle, D. J.; Grubb, A.; Ohlsson, K. Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. Biochem. J. 1991, 273, 621-626.
    • (1991) Biochem. J. , vol.273 , pp. 621-626
    • Abrahamson, M.1    Mason, R.W.2    Hansson, H.3    Buttle, D.J.4    Grubb, A.5    Ohlsson, K.6
  • 6
    • 84985287392 scopus 로고
    • Assay systems and characterization of Pacific whiting (Merluccius productus) protease
    • An, H.; Seymour, T. A.; Wu, J. W.; Morrissey, M. T. Assay systems and characterization of Pacific whiting (Merluccius productus) protease. J. Food Sci. 1994, 59, 277-281.
    • (1994) J. Food Sci. , vol.59 , pp. 277-281
    • An, H.1    Seymour, T.A.2    Wu, J.W.3    Morrissey, M.T.4
  • 7
    • 0020541585 scopus 로고
    • Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum
    • Anastasi, A.; Brown, M. A.; Kembhavi, A. A.; Nicklin, M. J. H.; Sayers, C. A.; Sunter, D.; Barrett, A. J. Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Biochem. J. 1983, 211, 129-138.
    • (1983) Biochem. J. , vol.211 , pp. 129-138
    • Anastasi, A.1    Brown, M.A.2    Kembhavi, A.A.3    Nicklin, M.J.H.4    Sayers, C.A.5    Sunter, D.6    Barrett, A.J.7
  • 9
    • 0028903615 scopus 로고
    • Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain
    • Auerswald, E. A.; Nagler, D. K.; Assfalg-Machleidt, I.; Stubbs, M. T.; Werner, M.; Hans, F. Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain. FEBS Lett. 1995, 361, 179-184.
    • (1995) FEBS Lett. , vol.361 , pp. 179-184
    • Auerswald, E.A.1    Nagler, D.K.2    Assfalg-Machleidt, I.3    Stubbs, M.T.4    Werner, M.5    Hans, F.6
  • 10
    • 0023268643 scopus 로고
    • The cystatins: A new class of peptidase inhibitors
    • Barrett, A. J. The cystatins: a new class of peptidase inhibitors. Trends Biochem. Sci. 1987, 12, 193-196.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 193-196
    • Barrett, A.J.1
  • 12
    • 0032029354 scopus 로고    scopus 로고
    • Production of rat salivary cystatin S variant polypeptides in Escherichia coli
    • Bedi, G. S.; Zhou, T.; Bedi, S. K. Production of rat salivary cystatin S variant polypeptides in Escherichia coli. Arch. Oral. Biol. 1998, 43, 173-182.
    • (1998) Arch. Oral. Biol. , vol.43 , pp. 173-182
    • Bedi, G.S.1    Zhou, T.2    Bedi, S.K.3
  • 13
    • 0025057074 scopus 로고
    • Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain a, and ficin
    • Bjork, I.; Ylinenjarivi, K. Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain a, and ficin. Biochemistry 1990, 29, 1770-1776.
    • (1990) Biochemistry , vol.29 , pp. 1770-1776
    • Bjork, I.1    Ylinenjarivi, K.2
  • 14
    • 0026670859 scopus 로고
    • Different roles of the two disulfide bonds of the cysteine proteinase inhibitor, chicken cystatin, for the conformation of the active protein
    • Bjork, I.; Ylinenjarvi, K. Different roles of the two disulfide bonds of the cysteine proteinase inhibitor, chicken cystatin, for the conformation of the active protein. Biochemistry 1992, 31, 8597-9602.
    • (1992) Biochemistry , vol.31 , pp. 8597-9602
    • Bjork, I.1    Ylinenjarvi, K.2
  • 15
    • 0024556990 scopus 로고
    • Kinetics of binding of chicken cystatin to papain
    • Bjork, I.; Alriksson, E.; Ylinenjarivi, K. Kinetics of binding of chicken cystatin to papain. Biochemistry 1989, 28, 1568-1573.
    • (1989) Biochemistry , vol.28 , pp. 1568-1573
    • Bjork, I.1    Alriksson, E.2    Ylinenjarivi, K.3
  • 16
    • 0028220189 scopus 로고
    • Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes
    • Bjork, I.; Pol, E.; Raub-Segall, E.; Abrahamson, M.; Rowan, A. D.; Mort, J. S. Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes. Biochem. J. 1994, 299, 219-225.
    • (1994) Biochem. J. , vol.299 , pp. 219-225
    • Bjork, I.1    Pol, E.2    Raub-Segall, E.3    Abrahamson, M.4    Rowan, A.D.5    Mort, J.S.6
  • 17
    • 0028937017 scopus 로고
    • Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases
    • Bjork, I.; Brieditis, I.; Abrahamson, M. Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases. Biochem. J. 1995, 306, 513-518.
    • (1995) Biochem. J. , vol.306 , pp. 513-518
    • Bjork, I.1    Brieditis, I.2    Abrahamson, M.3
  • 18
    • 0028587077 scopus 로고
    • Biological activities and secondary structures of variant forms of human salivary cystatin SN produced in Escherichia coli
    • Bobek, L. A.; Ramasubbu, N.; Wang, X.; Weaver, T. R.; Levine, M. J. Biological activities and secondary structures of variant forms of human salivary cystatin SN produced in Escherichia coli. Gene 1994, 151, 303-308.
    • (1994) Gene , vol.151 , pp. 303-308
    • Bobek, L.A.1    Ramasubbu, N.2    Wang, X.3    Weaver, T.R.4    Levine, M.J.5
  • 19
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W.; Engh, R. A.; Musil, D.; Thiele, U.; Huber, R.; Karshikov, A.; Brzin, J.; Kos, J.; Turk, V. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 1988, 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.A.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 20
    • 0021053487 scopus 로고
    • Protein inhibitors of cysteine proteinases I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphnuclear granulocytes
    • Brzin, J.; Kopitar, M.; Turk, V. Protein inhibitors of cysteine proteinases I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphnuclear granulocytes. Hoppe-Seyler Z. Biol. Chem. 1983, 364, 1475-1478.
    • (1983) Hoppe-Seyler Z. Biol. Chem. , vol.364 , pp. 1475-1478
    • Brzin, J.1    Kopitar, M.2    Turk, V.3
  • 21
    • 0343089728 scopus 로고
    • Low molecular mass protein inhibitor of cysteine proteinases from soybean
    • Brzin, J.; Ritonja, A.; Popovic, T.; Turk, V. Low molecular mass protein inhibitor of cysteine proteinases from soybean. Hoppe-Seyler Z. Biol. Chem. 1990, 377, 167-170.
    • (1990) Hoppe-Seyler Z. Biol. Chem. , vol.377 , pp. 167-170
    • Brzin, J.1    Ritonja, A.2    Popovic, T.3    Turk, V.4
  • 22
    • 0024971526 scopus 로고
    • Chicken egg white cystatin. Molecular cloning, nucleotide sequence, and tissue distribution
    • Colella, R.; Sakaguchi, Y.; Nagase, H.; Bird, J. W. Chicken egg white cystatin. Molecular cloning, nucleotide sequence, 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
  • 23
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman, A. I.; Prinz, W. A.; Belin, D.; Beckwith, J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 1993, 262, 1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 24
    • 0024426162 scopus 로고
    • Bacterial expression of human cysteine proteinase inhibitor stefin A
    • Fong, D.; Kartasova, T.; Sloane, B. F.; Chan, M. M. Y. Bacterial expression of human cysteine proteinase inhibitor stefin A. FEBS Lett. 1989, 257, 55-58.
    • (1989) FEBS Lett. , vol.257 , pp. 55-58
    • Fong, D.1    Kartasova, T.2    Sloane, B.F.3    Chan, M.M.Y.4
  • 25
    • 0014278378 scopus 로고
    • Ficin and papain inhibitor from chicken egg white
    • Fossum, K.; Whitaker, J. R. Ficin and papain inhibitor from chicken egg white. Arch. Biochem. Biophys. 1968, 125, 367-375.
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 367-375
    • Fossum, K.1    Whitaker, J.R.2
  • 26
    • 0032497910 scopus 로고    scopus 로고
    • Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C
    • Gerhartz, B.; Ekiel, I.; Abrahamson, M. Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C. Biochemistry 1998, 37, 17309-17317.
    • (1998) Biochemistry , vol.37 , pp. 17309-17317
    • Gerhartz, B.1    Ekiel, I.2    Abrahamson, M.3
  • 27
    • 0021141631 scopus 로고
    • The disulphide bridge of human cystatin C (y-trace) and chicken cystatin
    • Grubb, A.; Lofberg, H.; Barrett, A. J. The disulphide bridge of human cystatin C (y-trace) and chicken cystatin. FEBS Lett. 1984, 270, 370-374.
    • (1984) FEBS Lett. , vol.270 , pp. 370-374
    • Grubb, A.1    Lofberg, H.2    Barrett, A.J.3
  • 28
    • 0018938777 scopus 로고
    • Plasmid screening at high colony density
    • Hanahan, D.; Meselson, M. Plasmid screening at high colony density. Gene 1980, 10, 63-67.
    • (1980) Gene , vol.10 , pp. 63-67
    • Hanahan, D.1    Meselson, M.2
  • 29
    • 0023733116 scopus 로고
    • Cloning a synthetic gene for human stefin B and its expression in E. coli
    • Jerala, R.; Trstenjak, M.; Lenarcic, B.; Turk, V. Cloning a synthetic gene for human stefin B and its expression in E. coli. FEBS Lett. 1988, 239, 41-44.
    • (1988) FEBS Lett. , vol.239 , pp. 41-44
    • Jerala, R.1    Trstenjak, M.2    Lenarcic, B.3    Turk, V.4
  • 30
    • 0040854423 scopus 로고    scopus 로고
    • Effect of Cathepsins B, L, L-like and Calpain on the Protein Degradation of Surimi
    • Xiong, Y. L., Ho, C. T., Shahidi, F., Eds.; ACS Symposium Series 215; Kluwer Academic/Plenum Publishers: New York; Chapter 26
    • Jiang, S. T.; Chen, G. H. Effect of Cathepsins B, L, L-like and Calpain on the Protein Degradation of Surimi. In Quality Attributes of Muscle Foods; Xiong, Y. L., Ho, C. T., Shahidi, F., Eds.; ACS Symposium Series 215; Kluwer Academic/Plenum Publishers: New York, 1998; Chapter 26, pp 393-405.
    • (1998) Quality Attributes of Muscle Foods , pp. 393-405
    • Jiang, S.T.1    Chen, G.H.2
  • 31
    • 33751158499 scopus 로고
    • Purification and characterization of cathepsin B from ordinary muscle of mackerel (Scomber australasicus)
    • Jiang, S. T.; Lee, J. J.; Chen, H. C. Purification and characterization of cathepsin B from ordinary muscle of mackerel (Scomber australasicus). J. Agric. Food Chem. 1994, 42, 1073-1079.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1073-1079
    • Jiang, S.T.1    Lee, J.J.2    Chen, H.C.3
  • 32
    • 0030968742 scopus 로고    scopus 로고
    • Mackerel cathepsins B and L effects on thermal degradation of surimi
    • Jiang, S. T.; Lee, B. L.; Tsao, C. Y.; Lee, J. J. Mackerel cathepsins B and L effects on thermal degradation of surimi. J. Food Sci. 1997, 62, 310-315.
    • (1997) J. Food Sci. , vol.62 , pp. 310-315
    • Jiang, S.T.1    Lee, B.L.2    Tsao, C.Y.3    Lee, J.J.4
  • 33
    • 0024579707 scopus 로고
    • Studies on chemical synthesis of human cystatin A gene and its expression in E. coli
    • Kaji, H.; Kumagai, I.; Takeda, A.; Miura, K. I.; Samejima, T. Studies on chemical synthesis of human cystatin A gene and its expression in E. coli. J. Biochem. 1989, 105, 143-147.
    • (1989) J. Biochem. , vol.105 , pp. 143-147
    • Kaji, H.1    Kumagai, I.2    Takeda, A.3    Miura, K.I.4    Samejima, T.5
  • 35
    • 0023693249 scopus 로고
    • Total synthesis of the cystatin α-gene and its expression in E. coli
    • Katunuma, N.; Yamato, M.; Kominami, E.; Ike, Y. Total synthesis of the cystatin α-gene and its expression in E. coli. FEBS Lett. 1988, 238, 116-118.
    • (1988) FEBS Lett. , vol.238 , pp. 116-118
    • Katunuma, N.1    Yamato, M.2    Kominami, E.3    Ike, Y.4
  • 36
    • 0015982934 scopus 로고
    • Effect of papain inhibitor from chicken egg white on cathepsin B1
    • Keilova, H.; Tomasek, V. Effect of papain inhibitor from chicken egg white on cathepsin B1. Biochim. Biophys. Acta 1974, 334, 179-186.
    • (1974) Biochim. Biophys. Acta , vol.334 , pp. 179-186
    • Keilova, H.1    Tomasek, V.2
  • 38
    • 77957773738 scopus 로고
    • Purification and characterization of proteinases identified as cathepsin L and L-like (58 kDa) from mackerel (Scomber australasicus)
    • Lee, J. J.; Chen, H. C.; Jiang, S. T. Purification and characterization of proteinases identified as cathepsin L and L-like (58 kDa) from mackerel (Scomber australasicus). Biosci., Biotechnol., Biochem. 1993, 57, 1470-1476.
    • (1993) Biosci., Biotechnol., Biochem. , vol.57 , pp. 1470-1476
    • Lee, J.J.1    Chen, H.C.2    Jiang, S.T.3
  • 39
    • 0034073998 scopus 로고    scopus 로고
    • Purification and characterization of low molecular weight kininogen from pig plasma
    • Lee, J. J.; Tzeng, S. S.; Jiang, S. T. Purification and characterization of low molecular weight kininogen from pig plasma. J. Food Sci. 2000, 65, 81-86.
    • (2000) J. Food Sci. , vol.65 , pp. 81-86
    • Lee, J.J.1    Tzeng, S.S.2    Jiang, S.T.3
  • 40
    • 0023801371 scopus 로고
    • Interaction of the cysteine proteinase inhibitor chicken cystatin with papain
    • Lindahl, P.; Alriksson, E.; Jornvall, H.; Bjork, I. Interaction of the cysteine proteinase inhibitor chicken cystatin with papain. Biochemistry 1988, 27, 5074-5082.
    • (1988) Biochemistry , vol.27 , pp. 5074-5082
    • Lindahl, P.1    Alriksson, E.2    Jornvall, H.3    Bjork, I.4
  • 41
    • 0026570448 scopus 로고
    • Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
    • Lindahl, P.; Abrahamson, M.; Bjork, I. Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin. Biochem. J. 1992a, 281, 49-55.
    • (1992) Biochem. J. , vol.281 , pp. 49-55
    • Lindahl, P.1    Abrahamson, M.2    Bjork, I.3
  • 42
    • 0026744734 scopus 로고
    • Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin
    • Lindahl, P.; Nycander, M.; Ylinenjarvi, K.; Pol, E.; Bjork, I. Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin. Biochem. J. 1992b, 286, 165-171.
    • (1992) Biochem. J. , vol.286 , pp. 165-171
    • Lindahl, P.1    Nycander, M.2    Ylinenjarvi, K.3    Pol, E.4    Bjork, I.5
  • 43
    • 0024570048 scopus 로고
    • Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor
    • Machleidt, W.; Thiele, U.; Laber, B.; Assfalg-Machleidt, I.; Esterl, A.; Wiegand, G.; Kos, J.; Turk., V.; Bode, W. Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor. FEBS Lett. 1989, 243, 234-238.
    • (1989) FEBS Lett. , vol.243 , pp. 234-238
    • Machleidt, W.1    Thiele, U.2    Laber, B.3    Assfalg-Machleidt, I.4    Esterl, A.5    Wiegand, G.6    Kos, J.7    Turk, V.8    Bode, W.9
  • 45
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear backgroung at nanogram sensitivity using coomassie brilliant blue G-250 and R-250
    • Neuhoff, V.; Arold, N.; Toube, D.; Ehrhardt, W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear backgroung at nanogram sensitivity using coomassie brilliant blue G-250 and R-250. Electrophoresis 1988, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Toube, D.3    Ehrhardt, W.4
  • 46
    • 0021676681 scopus 로고
    • Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin
    • Nicklin, M. J. H.; Barrett, A. J. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 1984, 223, 245-253.
    • (1984) Biochem. J. , vol.223 , pp. 245-253
    • Nicklin, M.J.H.1    Barrett, A.J.2
  • 47
    • 0025109431 scopus 로고
    • Inhibition of cysteine proteinases by a protein inhibitor from potato
    • Rowan, A. D.; Brzin, J.; Buttle, D. J.; Barrett, A. J. Inhibition of cysteine proteinases by a protein inhibitor from potato. FEBS Lett. 1990, 269, 328-330.
    • (1990) FEBS Lett. , vol.269 , pp. 328-330
    • Rowan, A.D.1    Brzin, J.2    Buttle, D.J.3    Barrett, A.J.4
  • 49
    • 0029338406 scopus 로고
    • Expression of a functional rat salivary cystatin S polypeptide in Escherichia coli
    • Sharma, A.; O'Connell, B. C.; Tabak, L. A.; Bedi, G. S. Expression of a functional rat salivary cystatin S polypeptide in Escherichia coli. Arch. Oral. Biol. 1995, 40, 639-644.
    • (1995) Arch. Oral. Biol. , vol.40 , pp. 639-644
    • Sharma, A.1    O'Connell, B.C.2    Tabak, L.A.3    Bedi, G.S.4
  • 51
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs, M. T.; Laber, B.; Bode, W.; Huber, R.; Jerala, R.; Lenarcic, B.; Turk, V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 1990, 9, 1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 53
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk, V.; Bode, W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 1991, 285, 213-219.
    • (1991) FEBS Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 54
    • 0000758264 scopus 로고
    • Effects of additives on proteolytic and functional properties of arrowtooth flounder surimi
    • Wasson, D. H.; Reppond, K. D.; Babbitt, J. K.; French, J. S. Effects of additives on proteolytic and functional properties of arrowtooth flounder surimi. J. Aquat. Food Prod. Technol. 1992a, 1 (3/4), 147-165.
    • (1992) J. Aquat. Food Prod. Technol. , vol.1 , Issue.3-4 , pp. 147-165
    • Wasson, D.H.1    Reppond, K.D.2    Babbitt, J.K.3    French, J.S.4
  • 55
    • 84952513849 scopus 로고
    • Characterization of a heat stable protease from arrowtooth flounder, Atheresthes stomias
    • Wasson, D.; Babbitt, J. K.; French, J. S. Characterization of a heat stable protease from arrowtooth flounder, Atheresthes stomias. J. Aquat. Food Prod. Technol. 1992b, 1 (3/4), 167-182.
    • (1992) J. Aquat. Food Prod. Technol. , vol.1 , Issue.3-4 , pp. 167-182
    • Wasson, D.1    Babbitt, J.K.2    French, J.S.3
  • 56
    • 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
  • 57
    • 0030711080 scopus 로고    scopus 로고
    • Thermal denaturation of human cystatin C and two of its variants; comparison to chicken cystatin
    • Zerovnik, E.; Cimerman, N.; Kos, J.; Turk, V.; Lohner, K. Thermal denaturation of human cystatin C and two of its variants; comparison to chicken cystatin. Biol. Chem. 1997, 378, 1199-1203.
    • (1997) Biol. Chem. , vol.378 , pp. 1199-1203
    • Zerovnik, E.1    Cimerman, N.2    Kos, J.3    Turk, V.4    Lohner, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.