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Volumn 7, Issue 3, 1998, Pages 637-648

Role of the amino-terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides

Author keywords

Amidolytic activity; Fragment complementation; N terminal region of streptokinase; Plasminogen; Plasminogen activation; Streptokinase; Substrate plasminogen

Indexed keywords

PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; STREPTOKINASE; SYNTHETIC PEPTIDE;

EID: 0031911761     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070313     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen CB, Scheraga HA. 1975. Experimental and theoretical aspects of protein folding. Adv Protein Chem 29:205-299.
    • (1975) Adv Protein Chem , vol.29 , pp. 205-299
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 3
    • 0017184389 scopus 로고
    • A rapid method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM. 1976. A rapid method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Biochemistry 72:248-254.
    • (1976) Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0019719303 scopus 로고
    • Recent advances in the chemistry of the fibrinolytic system
    • Castellino FJ. 1981. Recent advances in the chemistry of the fibrinolytic system. Chem Rev 81:431-446.
    • (1981) Chem Rev , vol.81 , pp. 431-446
    • Castellino, F.J.1
  • 5
    • 0019761469 scopus 로고
    • Semisynthetic proteins
    • Chaiken IM. 1981. Semisynthetic proteins. CRC Crit Rev Biochem 11:255-330.
    • (1981) CRC Crit Rev Biochem , vol.11 , pp. 255-330
    • Chaiken, I.M.1
  • 6
    • 0030448926 scopus 로고    scopus 로고
    • Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance
    • Conejero-Lara F, Parrado J, Azuaga AI, Smith RAG, Ponting CP, Dobson CM. 1996. Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance. Protein Sci 5:2583-2591.
    • (1996) Protein Sci , vol.5 , pp. 2583-2591
    • Conejero-Lara, F.1    Parrado, J.2    Azuaga, A.I.3    Smith, R.A.G.4    Ponting, C.P.5    Dobson, C.M.6
  • 7
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • Deutsch DG, Mertz ET. 1970. Plasminogen: Purification from human plasma by affinity chromatography. Science 170:1095-1096.
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 9
    • 0027404489 scopus 로고
    • Streptokinase and human fibronectin share a common epitope: Implications for regulation of fibrinolysis and rheumatoid arthritis
    • Gonzalez-Gronow M, Enghild JJ, Pizzo SV. 1993. Streptokinase and human fibronectin share a common epitope: Implications for regulation of fibrinolysis and rheumatoid arthritis. Biochim Biophys Acta 1180:283-288.
    • (1993) Biochim Biophys Acta , vol.1180 , pp. 283-288
    • Gonzalez-Gronow, M.1    Enghild, J.J.2    Pizzo, S.V.3
  • 10
    • 0026607185 scopus 로고
    • Third international study of infarct survival collaborative group. A randomized comparison of streptokinase vs tissue plasminogen activator vs anistreplase and of aspirin plus heparin vs aspirin alone among 41,229 cases of suspected acute myocardial infarction
    • ISIS-3. 1992. Third international study of infarct survival collaborative group. A randomized comparison of streptokinase vs tissue plasminogen activator vs anistreplase and of aspirin plus heparin vs aspirin alone among 41,229 cases of suspected acute myocardial infarction. The Lancet 339:753-781.
    • (1992) The Lancet , vol.339 , pp. 753-781
  • 12
    • 0024791634 scopus 로고
    • Site-specific alteration of Gly-24 in streptokinase: Its effect on plasminogen activation
    • Lee RB, Park KS, Kim HJ, Byun MS. 1989. Site-specific alteration of Gly-24 in streptokinase: Its effect on plasminogen activation. Biochem Biophys Res Commun 165:1085-1090.
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 1085-1090
    • Lee, R.B.1    Park, K.S.2    Kim, H.J.3    Byun, M.S.4
  • 13
    • 0030452422 scopus 로고    scopus 로고
    • Mutation of lysines in a plasminogen binding region of streptokinase identifies residues important for generating a functional activator complex
    • Lin FL, Oeun S, Houng A, Reed GL. 1996. Mutation of lysines in a plasminogen binding region of streptokinase identifies residues important for generating a functional activator complex. Biochemistry 35:16879-16885.
    • (1996) Biochemistry , vol.35 , pp. 16879-16885
    • Lin, F.L.1    Oeun, S.2    Houng, A.3    Reed, G.L.4
  • 14
    • 0021245163 scopus 로고
    • Streptokinase: Cloning, expression and excretion by Escherichia coli
    • Malke H, Ferretti JJ. 1984. Streptokinase: Cloning, expression and excretion by Escherichia coli. Proc Natl Acad Sci USA 81:3557-3561.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3557-3561
    • Malke, H.1    Ferretti, J.J.2
  • 15
    • 0021885514 scopus 로고
    • Nucleotide sequence of the streptokinase gene from Streptococcal equisimilis H46A
    • Malke H, Roe B, Ferretti JJ. 1985. Nucleotide sequence of the streptokinase gene from Streptococcal equisimilis H46A. Gene 34:357-367.
    • (1985) Gene , vol.34 , pp. 357-367
    • Malke, H.1    Roe, B.2    Ferretti, J.J.3
  • 16
    • 0002550822 scopus 로고
    • Streptokinase: Expression of altered forms
    • Ferretti JJ, Curtis R. III, eds. Washington DC: American Society for Microbiology
    • Malke H, Roe B, Ferretti JJ. 1987. Streptokinase: Expression of altered forms. In: Ferretti JJ, Curtis R. III, eds. Streptococcal genetics. Washington DC: American Society for Microbiology. pp 143-149.
    • (1987) Streptococcal Genetics , pp. 143-149
    • Malke, H.1    Roe, B.2    Ferretti, J.J.3
  • 17
    • 0027742954 scopus 로고
    • Recombinant streptokinase: Opportunity for an improved agent
    • Marder VJ. 1993. Recombinant streptokinase: Opportunity for an improved agent. Blood coagulation and fibrinolysis 4:1039-1040.
    • (1993) Blood Coagulation and Fibrinolysis , vol.4 , pp. 1039-1040
    • Marder, V.J.1
  • 18
    • 0010147318 scopus 로고
    • The interaction of streptokinase with plasminogen: Functional properties of the activated enzyme
    • Markus G, Werkheiser WC. 1964. The interaction of streptokinase with plasminogen: Functional properties of the activated enzyme. J Biol Chem 239:2637-2643.
    • (1964) J Biol Chem , vol.239 , pp. 2637-2643
    • Markus, G.1    Werkheiser, W.C.2
  • 19
    • 0015213796 scopus 로고
    • The mechanism of activation of human plasminogen by streptokinase
    • McClintock DK, Bell PH. 1971. The mechanism of activation of human plasminogen by streptokinase. Biochem Biophys Res Commun 45:694-702.
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 694-702
    • McClintock, D.K.1    Bell, P.H.2
  • 20
    • 0030925283 scopus 로고    scopus 로고
    • Mapping of the plasminogen binding site of streptokinase with short synthetic peptides
    • Nihalani D, Raghava GPS, Sahni G. 1997. Mapping of the plasminogen binding site of streptokinase with short synthetic peptides. Protein Sci 6:1284-1292.
    • (1997) Protein Sci , vol.6 , pp. 1284-1292
    • Nihalani, D.1    Raghava, G.P.S.2    Sahni, G.3
  • 21
    • 0029620638 scopus 로고
    • Streptokinase contains two independent plasminogen-binding sites
    • Nihalani D, Sahni G. 1995. Streptokinase contains two independent plasminogen-binding sites. Biochem Biophys Res Commun 217:1245-1254.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1245-1254
    • Nihalani, D.1    Sahni, G.2
  • 22
    • 0000811883 scopus 로고
    • Protein engineering by chemical means
    • Offord JE. 1987. Protein engineering by chemical means. Protein Eng 1:151-157.
    • (1987) Protein Eng , vol.1 , pp. 151-157
    • Offord, J.E.1
  • 23
    • 0029873754 scopus 로고    scopus 로고
    • The domain organization of streptokinase: Nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments
    • Parrado J, Conejero-Lara F, Smith RAG, Marshall JM, Ponting CP, Dobson CM. 1996. The domain organization of streptokinase: Nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments. Protein Sci 5:693-704.
    • (1996) Protein Sci , vol.5 , pp. 693-704
    • Parrado, J.1    Conejero-Lara, F.2    Smith, R.A.G.3    Marshall, J.M.4    Ponting, C.P.5    Dobson, C.M.6
  • 26
    • 0015522766 scopus 로고
    • Mechanism of activation human plasminogen by streptokinase
    • Reddy KNN, Markus G. 1972. Mechanism of activation human plasminogen by streptokinase. J Biol Chem 247:1683-1691.
    • (1972) J Biol Chem , vol.247 , pp. 1683-1691
    • Reddy, K.N.N.1    Markus, G.2
  • 27
    • 0029079778 scopus 로고
    • Identification of a plasminogen binding region in streptokinase that is necessary for the creation of a functional streptokinase-plasminogen activator complex
    • Reed GL, Lin LF, Parhami-Seren B, Kussie P. 1995. Identification of a plasminogen binding region in streptokinase that is necessary for the creation of a functional streptokinase-plasminogen activator complex. Biochemistry 34:10266-10271.
    • (1995) Biochemistry , vol.34 , pp. 10266-10271
    • Reed, G.L.1    Lin, L.F.2    Parhami-Seren, B.3    Kussie, P.4
  • 29
    • 0026598469 scopus 로고
    • Purification of streptokinase by affinity chromatography on immobilized acylated human plasminogen
    • Rodriguez P, Hernandez L, Munoz E, Castro A, Fuente de la J, Herrera L. 1992. Purification of streptokinase by affinity chromatography on immobilized acylated human plasminogen. Biotechniques 12:424-427.
    • (1992) Biotechniques , vol.12 , pp. 424-427
    • Rodriguez, P.1    Hernandez, L.2    Munoz, E.3    Castro, A.4    De La Fuente, J.5    Herrera, L.6
  • 32
    • 0030064503 scopus 로고    scopus 로고
    • ATP-regulated activity of the plasmin-streptokinase complex: A novel mechanism involving phosphorylation of streptokinase
    • Serrano RL, Rodriguez P, Pizzo SV, Gonzalez-Gronow M. 1996. ATP-regulated activity of the plasmin-streptokinase complex: A novel mechanism involving phosphorylation of streptokinase. Biochem J 313:171-177.
    • (1996) Biochem J , vol.313 , pp. 171-177
    • Serrano, R.L.1    Rodriguez, P.2    Pizzo, S.V.3    Gonzalez-Gronow, M.4
  • 33
    • 0027985626 scopus 로고
    • Function of streptokinase fragments in plasminogen activation
    • Shi GY, Chang BI, Chen SM, Wu DH, Wu HL. 1994. Function of streptokinase fragments in plasminogen activation. Biochem J 304:235-241.
    • (1994) Biochem J , vol.304 , pp. 235-241
    • Shi, G.Y.1    Chang, B.I.2    Chen, S.M.3    Wu, D.H.4    Wu, H.L.5
  • 34
    • 0017126765 scopus 로고
    • Interaction of streptokinase with plasminogen
    • Siefring GE, Castellino FJ. 1976. Interaction of streptokinase with plasminogen. J Biol Chem 251:3913-3920.
    • (1976) J Biol Chem , vol.251 , pp. 3913-3920
    • Siefring, G.E.1    Castellino, F.J.2
  • 35
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier FW. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol 219:37-44.
    • (1991) J Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 36
    • 0018898952 scopus 로고
    • Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37°C
    • Wohl RC, Summaria L, Robbins KC. 1980. Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37°C. J Biol Chem 255:2005-2013.
    • (1980) J Biol Chem , vol.255 , pp. 2005-2013
    • Wohl, R.C.1    Summaria, L.2    Robbins, K.C.3


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