메뉴 건너뛰기




Volumn 27, Issue 8, 2006, Pages 822-831

Detailed Biochemical Characterization of Human Placental Cystatin (HPC)

Author keywords

Amino acid sequence; CD spectroscopy; Human placental cystatin; Immunodiffusion; Kinetics of inhibition

Indexed keywords

BROMELAIN; CARBOHYDRATE; CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; DISULFIDE; FICIN; GLYCINE; HIGH MOLECULAR WEIGHT KININOGEN; PAPAIN; PLACENTA PROTEIN; STEFIN A;

EID: 33745225232     PISSN: 01434004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.placenta.2005.09.005     Document Type: Article
Times cited : (14)

References (75)
  • 1
    • 0022896891 scopus 로고
    • The Cystatins: a diverse superfamily of cysteine peptidase inhibitors
    • Barrett A.J. The Cystatins: a diverse superfamily of cysteine peptidase inhibitors. Biomed Biochim Acta 45 11-12 (1986) 1363-1374
    • (1986) Biomed Biochim Acta , vol.45 , Issue.11-12 , pp. 1363-1374
    • Barrett, A.J.1
  • 2
    • 0025022426 scopus 로고
    • Evolution of proteins in the cystatin superfamily
    • Rawlings N.D., and Barrett A.J. Evolution of proteins in the cystatin superfamily. J Mol Biol 30 (1990) 60-71
    • (1990) J Mol Biol , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barrett, A.J.2
  • 7
    • 0027210445 scopus 로고
    • Cystatin C-CST3 the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA) and other members of the cystatin gene family are clustered on chromosome 20
    • Schnittger S., Gopal Rao V.V.N., Abrahamson M., and Hansmann I. Cystatin C-CST3 the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA) and other members of the cystatin gene family are clustered on chromosome 20. Genomics 16 (1993) 50-55
    • (1993) Genomics , vol.16 , pp. 50-55
    • Schnittger, S.1    Gopal Rao, V.V.N.2    Abrahamson, M.3    Hansmann, I.4
  • 9
    • 0024227598 scopus 로고
    • Human cysteine proteinases inhibitors: isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhages
    • Abrahamson M. Human cysteine proteinases inhibitors: isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhages. Scand J Clin Lab Invest 48 (1988) 21-31
    • (1988) Scand J Clin Lab Invest , vol.48 , pp. 21-31
    • Abrahamson, M.1
  • 10
    • 0023268643 scopus 로고
    • Cystatins: a new class of peptidase inhibitors
    • Barrett A.J. Cystatins: a new class of peptidase inhibitors. Trends Biochem Sci 12 (1984) 193-196
    • (1984) Trends Biochem Sci , vol.12 , pp. 193-196
    • Barrett, A.J.1
  • 11
    • 0019282838 scopus 로고
    • Pathophysiological interpretation of kinetic constants of protease inhibitors
    • Bieth J.G. Pathophysiological interpretation of kinetic constants of protease inhibitors. Bull Eur Physiopathol Respir 16 (1980) 183-197
    • (1980) Bull Eur Physiopathol Respir , vol.16 , pp. 183-197
    • Bieth, J.G.1
  • 12
    • 0028790320 scopus 로고
    • Factors influencing serum levels and peritoneal clearances of low molecular weight proteins in continuous ambulatory peritoneal dialysis
    • Kabanda A., Goffin E., and Bernard A. Factors influencing serum levels and peritoneal clearances of low molecular weight proteins in continuous ambulatory peritoneal dialysis. Kidney Int 48 (1995) 1946-1952
    • (1995) Kidney Int , vol.48 , pp. 1946-1952
    • Kabanda, A.1    Goffin, E.2    Bernard, A.3
  • 13
    • 0025772668 scopus 로고
    • Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, procathepsin L and a cathepsin L like 70 kDa proteinases
    • Delaisse J.M., Ledent P., and Vaes G. Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, procathepsin L and a cathepsin L like 70 kDa proteinases. Biochem J 279 (1991) 167-174
    • (1991) Biochem J , vol.279 , pp. 167-174
    • Delaisse, J.M.1    Ledent, P.2    Vaes, G.3
  • 14
    • 0025987727 scopus 로고
    • Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis
    • Trabandt A., Gay R.E., and Gay R.S. Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis. Arthritis Rheum 34 (1991) 444
    • (1991) Arthritis Rheum , vol.34 , pp. 444
    • Trabandt, A.1    Gay, R.E.2    Gay, R.S.3
  • 15
    • 0023922009 scopus 로고    scopus 로고
    • Enzymatically active cathepsin B dissociating from its inhibitor complexes is elevated in blood plasma of patients of septic shock and some malignant tumors
    • Assfalg-Machleidt I., Jochun M., Klaubert W., and Machleidt W. Enzymatically active cathepsin B dissociating from its inhibitor complexes is elevated in blood plasma of patients of septic shock and some malignant tumors. Biol Chem Hoppe Seyler 369 (1998) 263-269
    • (1998) Biol Chem Hoppe Seyler , vol.369 , pp. 263-269
    • Assfalg-Machleidt, I.1    Jochun, M.2    Klaubert, W.3    Machleidt, W.4
  • 16
    • 84940620175 scopus 로고
    • Cathepsin B-like proteinases as a marker for metastatic tumors cell variants
    • Koppel P., Baici A., Keist R., Matzku S., and Keller R. Cathepsin B-like proteinases as a marker for metastatic tumors cell variants. Exp Cell Biol 52 (1994) 293-299
    • (1994) Exp Cell Biol , vol.52 , pp. 293-299
    • Koppel, P.1    Baici, A.2    Keist, R.3    Matzku, S.4    Keller, R.5
  • 17
    • 0025105872 scopus 로고
    • Levels of neutrophil elastase and cathepsin B activities and cystatins in human sputum: relationship to inflammation
    • Buttle D.J., Burnett D., and Abrahamson M. Levels of neutrophil elastase and cathepsin B activities and cystatins in human sputum: relationship to inflammation. Scand J Clin Lab Invest 50 (1990) 509-516
    • (1990) Scand J Clin Lab Invest , vol.50 , pp. 509-516
    • Buttle, D.J.1    Burnett, D.2    Abrahamson, M.3
  • 18
    • 0024820274 scopus 로고
    • Detection of cathepsin B- and L-elastase, tryptase, trypsin and dipeptidyl peptidase IV like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin
    • Cox S.W., and Eley B.M. Detection of cathepsin B- and L-elastase, tryptase, trypsin and dipeptidyl peptidase IV like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. J Periodont Res 24 (1989) 353-361
    • (1989) J Periodont Res , vol.24 , pp. 353-361
    • Cox, S.W.1    Eley, B.M.2
  • 19
    • 13344269666 scopus 로고    scopus 로고
    • Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EMPI)
    • Pennacchio L.A., Lehesjoki A.E., Stone N.E., Willour V.L., Virtaneva K., Miao J., et al. Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EMPI). Science 271 (1996) 1731-1734
    • (1996) Science , vol.271 , pp. 1731-1734
    • Pennacchio, L.A.1    Lehesjoki, A.E.2    Stone, N.E.3    Willour, V.L.4    Virtaneva, K.5    Miao, J.6
  • 20
    • 0022406394 scopus 로고
    • Purification and characterization of a low molecular weight cysteine proteinases inhibitor from bovine muscle
    • Beige L., Ouali A., and Valin C. Purification and characterization of a low molecular weight cysteine proteinases inhibitor from bovine muscle. Biochem Biophys Acta 843 (1985) 269-273
    • (1985) Biochem Biophys Acta , vol.843 , pp. 269-273
    • Beige, L.1    Ouali, A.2    Valin, C.3
  • 21
    • 0020467150 scopus 로고
    • Human spleen cysteine proteinase inhibitor. Purification, fractionation in to isoelectric variants and some properties of the variants
    • Jarvinen M., and Rinnie A. Human spleen cysteine proteinase inhibitor. Purification, fractionation in to isoelectric variants and some properties of the variants. Biochem Biophys Acta 708 2 (1982) 210-217
    • (1982) Biochem Biophys Acta , vol.708 , Issue.2 , pp. 210-217
    • Jarvinen, M.1    Rinnie, A.2
  • 22
    • 0021346826 scopus 로고
    • Cystatin-like cysteine proteinases inhibitors from human liver
    • Green G.D.J., Kembhavi A.A., Davies M.E., and Barrett A.J. Cystatin-like cysteine proteinases inhibitors from human liver. Biochem J 218 (1984) 939-946
    • (1984) Biochem J , vol.218 , pp. 939-946
    • Green, G.D.J.1    Kembhavi, A.A.2    Davies, M.E.3    Barrett, A.J.4
  • 23
    • 0021053487 scopus 로고
    • Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Brzin J., Kopitar M., Turk V., and Machleidt M. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe Seyler's Z Physiol Chem 364 (1983) 1475
    • (1983) Hoppe Seyler's Z Physiol Chem , vol.364 , pp. 1475
    • Brzin, J.1    Kopitar, M.2    Turk, V.3    Machleidt, M.4
  • 24
    • 0021080396 scopus 로고
    • Protein inhibitors of cysteine proteinases II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Machleidt W., Borchart U., Fritz H., Brzin J., Ritonja A., and Turk V. Protein inhibitors of cysteine proteinases II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe Seyler's Z Physiol Chem 364 (1983) 1481-1486
    • (1983) Hoppe Seyler's Z Physiol Chem , vol.364 , pp. 1481-1486
    • Machleidt, W.1    Borchart, U.2    Fritz, H.3    Brzin, J.4    Ritonja, A.5    Turk, V.6
  • 25
    • 0020604495 scopus 로고
    • Amyloid fibril in hereditary cerebral haemorrhages with amyloidosis (HCHWA) is related to the gastro-entero-pancreatic neuroendocrine protein, gamma trace
    • Cohen D.H., Feiner H., Jenson O., and Frangione B. Amyloid fibril in hereditary cerebral haemorrhages with amyloidosis (HCHWA) is related to the gastro-entero-pancreatic neuroendocrine protein, gamma trace. J Exp Med 158 (1983) 653
    • (1983) J Exp Med , vol.158 , pp. 653
    • Cohen, D.H.1    Feiner, H.2    Jenson, O.3    Frangione, B.4
  • 26
    • 0021257265 scopus 로고
    • New proteinases inhibitors of cysteine proteinases in human saliva and salivary glands
    • Minakata K., and Asano M. New proteinases inhibitors of cysteine proteinases in human saliva and salivary glands. Hoppe Seyler's Z Physiol Chem 365 (1984) 399
    • (1984) Hoppe Seyler's Z Physiol Chem , vol.365 , pp. 399
    • Minakata, K.1    Asano, M.2
  • 27
    • 0021134636 scopus 로고
    • Cystatin S: a cysteine proteinases inhibitor of human saliva
    • Isemura S., Saitoh E., Isemura M., and Sanada K. Cystatin S: a cysteine proteinases inhibitor of human saliva. J Biochem 96 (1984) 1311
    • (1984) J Biochem , vol.96 , pp. 1311
    • Isemura, S.1    Saitoh, E.2    Isemura, M.3    Sanada, K.4
  • 28
    • 0017290367 scopus 로고
    • Human pregnancy associated plasma proteins during the post-partum period
    • Lin T.M., Halbert S.P., Spellacy W.N., and Gall S. Human pregnancy associated plasma proteins during the post-partum period. Am J Obstet Gynecol 124 4 (1976) 382-387
    • (1976) Am J Obstet Gynecol , vol.124 , Issue.4 , pp. 382-387
    • Lin, T.M.1    Halbert, S.P.2    Spellacy, W.N.3    Gall, S.4
  • 30
    • 9344222202 scopus 로고    scopus 로고
    • Studies on the interaction of papain with human placental cystatin by UV, fluorescence and CD spectroscopy
    • Rashid F., Baba S.P., Sharma S., and Bano B. Studies on the interaction of papain with human placental cystatin by UV, fluorescence and CD spectroscopy. Protein Pept Lett 11 6 (2004) 583-591
    • (2004) Protein Pept Lett , vol.11 , Issue.6 , pp. 583-591
    • Rashid, F.1    Baba, S.P.2    Sharma, S.3    Bano, B.4
  • 31
    • 85137966954 scopus 로고    scopus 로고
    • Rashid F, Sharma S, Bano B. Comparison of guanidine hydrochloride (GdnHCl) and urea denaturation on inactivation and unfolding of Human Placental Cystatin (HPC). Protein J 2005;24 (in press).
  • 32
    • 0000795704 scopus 로고
    • Crystalline soya bean trypsin inhibitor, general properties
    • Kunitz M. Crystalline soya bean trypsin inhibitor, general properties. J Physiol 30 (1947) 291
    • (1947) J Physiol , vol.30 , pp. 291
    • Kunitz, M.1
  • 34
    • 33745194502 scopus 로고
    • Tissue sulphydryl groups
    • Ellman R. Tissue sulphydryl groups. Biochem Methods 19 (1969) 446-451
    • (1969) Biochem Methods , vol.19 , pp. 446-451
    • Ellman, R.1
  • 36
    • 84873776231 scopus 로고
    • Diffusion in gel methods for immunological analysis II
    • Ouchterlony O. Diffusion in gel methods for immunological analysis II. Prog Allergy 6 (1962) 30-154
    • (1962) Prog Allergy , vol.6 , pp. 30-154
    • Ouchterlony, O.1
  • 37
    • 21044440593 scopus 로고    scopus 로고
    • Purification and characterization of kininogens from sheep plasma
    • Baba S.P., Zehra S., and Bano B. Purification and characterization of kininogens from sheep plasma. Protein J 24 2 (2005) 95-102
    • (2005) Protein J , vol.24 , Issue.2 , pp. 95-102
    • Baba, S.P.1    Zehra, S.2    Bano, B.3
  • 38
    • 23744439180 scopus 로고    scopus 로고
    • Biochemical and biophysical changes induced by fungicide sodium diethyl dithiocarbamate (SDD), in phytocystatin purified from Phaseolus mungo (Urd) - a commonly used Indian legume
    • Sharma S., Rashid F., and Bano B. Biochemical and biophysical changes induced by fungicide sodium diethyl dithiocarbamate (SDD), in phytocystatin purified from Phaseolus mungo (Urd) - a commonly used Indian legume. J Agric Food Chem 53 15 (2005) 6027-6034
    • (2005) J Agric Food Chem , vol.53 , Issue.15 , pp. 6027-6034
    • Sharma, S.1    Rashid, F.2    Bano, B.3
  • 39
    • 0017190667 scopus 로고
    • Enzyme immunoassay in diagnostic medicine - theory and practice
    • Voller A., Bidwell D.E., and Bartlett A. Enzyme immunoassay in diagnostic medicine - theory and practice. Bull World Health Organ 53 (1976) 55-65
    • (1976) Bull World Health Organ , vol.53 , pp. 55-65
    • Voller, A.1    Bidwell, D.E.2    Bartlett, A.3
  • 40
    • 9344247875 scopus 로고
    • Effect of inhibitors
    • Krupka R.M., and Laidler K.J. Effect of inhibitors. Can J Chem 51 (1959) 1268-1271
    • (1959) Can J Chem , vol.51 , pp. 1268-1271
    • Krupka, R.M.1    Laidler, K.J.2
  • 41
    • 0015327378 scopus 로고
    • A linear equation that describes the steady state kinetics of enzymes and sub-cellular particles interacting with tightly bound inhibitors
    • Henderson P.J.F. A linear equation that describes the steady state kinetics of enzymes and sub-cellular particles interacting with tightly bound inhibitors. Biochem J 127 (1972) 321-333
    • (1972) Biochem J , vol.127 , pp. 321-333
    • Henderson, P.J.F.1
  • 42
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman P., and Begg G. A protein sequenator. Eur J Biochem 1 (1967) 80-91
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 43
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157 (1982) 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 44
    • 0027722909 scopus 로고
    • Purification and characterization of a polymorphic low M(r) bovine muscle cysteine proteinase inhibitor: structural identity with fatty acid binding proteins
    • Zabari M., Berri M., Rouchon P., Zamora F., Tassy C., Ribadean Dumas B., et al. Purification and characterization of a polymorphic low M(r) bovine muscle cysteine proteinase inhibitor: structural identity with fatty acid binding proteins. Biochimie 75 (1993) 937-945
    • (1993) Biochimie , vol.75 , pp. 937-945
    • Zabari, M.1    Berri, M.2    Rouchon, P.3    Zamora, F.4    Tassy, C.5    Ribadean Dumas, B.6
  • 45
    • 0028936570 scopus 로고
    • Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases
    • Turk B., Ritonja A., Bjork I., Stoka V., Dolenc I., and Turk V. Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases. FEBS Lett 360 (1995) 101-105
    • (1995) FEBS Lett , vol.360 , pp. 101-105
    • Turk, B.1    Ritonja, A.2    Bjork, I.3    Stoka, V.4    Dolenc, I.5    Turk, V.6
  • 46
    • 0013769988 scopus 로고
    • Estimation of the molecular weights of protein by sephadex gel filtration
    • Andrews P. Estimation of the molecular weights of protein by sephadex gel filtration. Biochem J 91 (1964) 222-233
    • (1964) Biochem J , vol.91 , pp. 222-233
    • Andrews, P.1
  • 47
    • 0000221435 scopus 로고
    • A theory of gel filtration and its experimental verification
    • Laurent T.C., and Killander J. A theory of gel filtration and its experimental verification. J Chromatogr (1964) 317
    • (1964) J Chromatogr , pp. 317
    • Laurent, T.C.1    Killander, J.2
  • 48
    • 0021236724 scopus 로고
    • The place of human gamma - trace (cystatin C) amongst the cysteine proteinase inhibitors
    • Barrett A.J., Davies M.E., and Grubb A. The place of human gamma - trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem Biophys Res Commun 120 (1984) 631-636
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 631-636
    • Barrett, A.J.1    Davies, M.E.2    Grubb, A.3
  • 49
    • 0022555509 scopus 로고
    • Human low molecular weight kininogens contain three copies of a cystatin sequence that are divergent in structure and inhibitory activity for cysteine proteinases
    • Salvesen G., Parkes C., Abrahamson M., Grubb A., and Barrett A.J. Human low molecular weight kininogens contain three copies of a cystatin sequence that are divergent in structure and inhibitory activity for cysteine proteinases. Biochem J 234 (1986) 429-434
    • (1986) Biochem J , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 51
    • 0030890648 scopus 로고    scopus 로고
    • Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins
    • Ni J., Abrahamson M., Zhang M., and Fernandez M.M. Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. J Biol Chem 272 16 (1997) 10853-10858
    • (1997) J Biol Chem , vol.272 , Issue.16 , pp. 10853-10858
    • Ni, J.1    Abrahamson, M.2    Zhang, M.3    Fernandez, M.M.4
  • 52
    • 0032544743 scopus 로고    scopus 로고
    • Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor
    • Ni J., Fernandez M.A., and Danielsson. Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor. J Biol Chem 273 38 (1998) 24797-24804
    • (1998) J Biol Chem , vol.273 , Issue.38 , pp. 24797-24804
    • Ni, J.1    Fernandez, M.A.2    Danielsson3
  • 53
    • 0031030180 scopus 로고    scopus 로고
    • Identification, cloning and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
    • Sotiropoulou G., Anisowics A., and Sager R. Identification, cloning and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J Biol Chem 272 2 (1997) 903-910
    • (1997) J Biol Chem , vol.272 , Issue.2 , pp. 903-910
    • Sotiropoulou, G.1    Anisowics, A.2    Sager, R.3
  • 54
    • 0030804153 scopus 로고    scopus 로고
    • Protein proteinase inhibitors from avian egg whites
    • Saxena I., and Tayyab S. Protein proteinase inhibitors from avian egg whites. Cell Mol Life Sci 53 (1997) 13-23
    • (1997) Cell Mol Life Sci , vol.53 , pp. 13-23
    • Saxena, I.1    Tayyab, S.2
  • 55
    • 0030711080 scopus 로고    scopus 로고
    • Thermal denaturation of human cystatin C and two of its variants; comparison to chicken cystatin
    • Zerovnik E., Cimermann N., Kos J., Turk V., and Lohner K. Thermal denaturation of human cystatin C and two of its variants; comparison to chicken cystatin. Biol Chem 378 (1997) 1199-1203
    • (1997) Biol Chem , vol.378 , pp. 1199-1203
    • Zerovnik, E.1    Cimermann, N.2    Kos, J.3    Turk, V.4    Lohner, K.5
  • 56
    • 0347422215 scopus 로고
    • Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin
    • Barrett A.J., Fritz H., Grubb A., and Isemura S. Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. Biochem J 236 1 (1986) 311-312
    • (1986) Biochem J , vol.236 , Issue.1 , pp. 311-312
    • Barrett, A.J.1    Fritz, H.2    Grubb, A.3    Isemura, S.4
  • 58
    • 33745193205 scopus 로고
    • Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases
    • Balbin M., Hall A., Grubb A., Mason R.W., Lopez-otin C., and Abrahamson M. Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. J Biol Chem 223 (1994) 245-253
    • (1994) J Biol Chem , vol.223 , pp. 245-253
    • Balbin, M.1    Hall, A.2    Grubb, A.3    Mason, R.W.4    Lopez-otin, C.5    Abrahamson, M.6
  • 59
    • 0021676681 scopus 로고
    • Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg white cystatin
    • Nicklin M.J.H., and Barrett A.J. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg white cystatin. Biochem J 223 (1984) 245-253
    • (1984) Biochem J , vol.223 , pp. 245-253
    • Nicklin, M.J.H.1    Barrett, A.J.2
  • 60
    • 0022311385 scopus 로고
    • Molecular basis of intracellular regulation of thiol protease inhibitors
    • Katunuma N., and Kominami E. Molecular basis of intracellular regulation of thiol protease inhibitors. Curr Top Cell Regul (1985) 345-360
    • (1985) Curr Top Cell Regul , pp. 345-360
    • Katunuma, N.1    Kominami, E.2
  • 61
    • 0024345739 scopus 로고
    • Interaction of chicken cystatin within activated papains
    • Bjork I., and Ylinenjarvi K. Interaction of chicken cystatin within activated papains. Biochem J 260 (1989) 61-68
    • (1989) Biochem J , vol.260 , pp. 61-68
    • Bjork, I.1    Ylinenjarvi, K.2
  • 62
    • 0014955627 scopus 로고
    • Prediction of secondary structure of proteins by circular dichroism study
    • Jirgensons B. Prediction of secondary structure of proteins by circular dichroism study. Biochem Biophys Acta 200 (1970) 9-17
    • (1970) Biochem Biophys Acta , vol.200 , pp. 9-17
    • Jirgensons, B.1
  • 63
    • 0016169865 scopus 로고
    • Determination of secondary structure of protein by circular dichroism and optical rotatory dispersion
    • Chen Y.H., Yang J.T., and Martinez H.M. Determination of secondary structure of protein by circular dichroism and optical rotatory dispersion. Biochemistry 13 (1972) 3350-3359
    • (1972) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 64
    • 0021383515 scopus 로고
    • Cystatin - amino acid sequence and possible secondary structure
    • Schwabe C., Anstasi A., Crow H., Mc Donald J.K., and Barett A.J. Cystatin - amino acid sequence and possible secondary structure. Biochem J 217 (1984) 813-817
    • (1984) Biochem J , vol.217 , pp. 813-817
    • Schwabe, C.1    Anstasi, A.2    Crow, H.3    Mc Donald, J.K.4    Barett, A.J.5
  • 66
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with cysteine proteinase papain - a novel type of proteinase-inhibitor interaction
    • Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., et al. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with cysteine proteinase papain - a novel type of proteinase-inhibitor interaction. EMBO J 9 (1990) 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
  • 67
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth R.A., Giannini S., Higgins L.D., Conroy M.J., Hounslow A.M., Jerala M., et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J 20 (2001) 4774-4781
    • (2001) EMBO J , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, M.6
  • 68
    • 0028932002 scopus 로고
    • Role of disulphide linkages in structure and activity of proteinases inhibitor from horsegram (Dolichos biflorus)
    • Ramasarma P.R., Appu Rao A.G., and Rao D.R. Role of disulphide linkages in structure and activity of proteinases inhibitor from horsegram (Dolichos biflorus). Biochem Biophys Acta 1248 (1995) 35-42
    • (1995) Biochem Biophys Acta , vol.1248 , pp. 35-42
    • Ramasarma, P.R.1    Appu Rao, A.G.2    Rao, D.R.3
  • 70
    • 0021873218 scopus 로고
    • Complete amino acid sequence of bovine coldtrum low-Mr cysteine proteinases inhibitor
    • Hirado M., Tsunasawa S., Sakiyama F., Niinobe M., and Fujii S. Complete amino acid sequence of bovine coldtrum low-Mr cysteine proteinases inhibitor. FEBS Lett 186 (1985) 41-45
    • (1985) FEBS Lett , vol.186 , pp. 41-45
    • Hirado, M.1    Tsunasawa, S.2    Sakiyama, F.3    Niinobe, M.4    Fujii, S.5
  • 71
    • 0022444892 scopus 로고
    • Characterization of a new cysteine proteinases inhibitor from human saliva, cystatin SN, which is immunologically related to cystatin S
    • Isemura S., Saitoh E., and Sanada K. Characterization of a new cysteine proteinases inhibitor from human saliva, cystatin SN, which is immunologically related to cystatin S. FEBS Lett 198 (1986) 145-149
    • (1986) FEBS Lett , vol.198 , pp. 145-149
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 72
    • 0023944901 scopus 로고
    • Purification, molecular cloning and sequencing of salivary cystatin SA-1
    • Al-Hashmi I., Dickinson D.P., and Levine M.J. Purification, molecular cloning and sequencing of salivary cystatin SA-1. J Biol Chem 263 (1988) 9381-9387
    • (1988) J Biol Chem , vol.263 , pp. 9381-9387
    • Al-Hashmi, I.1    Dickinson, D.P.2    Levine, M.J.3
  • 73
    • 0024371672 scopus 로고
    • Amino acid sequence of an inducible cysteine proteinase inhibitor (cystatin) from submandibular glands of isoproterenol-treated rats
    • Bedi G.S. Amino acid sequence of an inducible cysteine proteinase inhibitor (cystatin) from submandibular glands of isoproterenol-treated rats. Arch Biochem Biophys 273 1 (1989) 245-253
    • (1989) Arch Biochem Biophys , vol.273 , Issue.1 , pp. 245-253
    • Bedi, G.S.1
  • 74
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine proteinases inhibitor from human amniotic fluid
    • Ritonja A., Machleidt W., and Barett A.J. Amino acid sequence of the intracellular cysteine proteinases inhibitor from human amniotic fluid. Biochem Biophys Res Commun 131 (1985) 1107
    • (1985) Biochem Biophys Res Commun , vol.131 , pp. 1107
    • Ritonja, A.1    Machleidt, W.2    Barett, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.