메뉴 건너뛰기




Volumn 5, Issue 4, 1996, Pages 693-704

The domain organization of streptokinase: Nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments

Author keywords

fibrinolysis; NMR; plasminogen; proteolytic fragmentation; streptokinase

Indexed keywords

STREPTOKINASE;

EID: 0029873754     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050414     Document Type: Article
Times cited : (54)

References (45)
  • 1
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup T, Mullertz S. 1952. The fibrin plate method for estimating fibrinolytic activity. Arch Biochem Biophys 40:346-351.
    • (1952) Arch Biochem Biophys , vol.40 , pp. 346-351
    • Astrup, T.1    Mullertz, S.2
  • 2
    • 0017353766 scopus 로고
    • Activation of human plasminogen by equimolar levels of streptokinase
    • Bajaj SP, Castellino FJ. 1977. Activation of human plasminogen by equimolar levels of streptokinase. J Biol Chem 252:492-498.
    • (1977) J Biol Chem , vol.252 , pp. 492-498
    • Bajaj, S.P.1    Castellino, F.J.2
  • 3
    • 0016237609 scopus 로고
    • A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex
    • Brockway WJ, Castellino FJ. 1974. A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex. Biochemistry 13:2063-2070.
    • (1974) Biochemistry , vol.13 , pp. 2063-2070
    • Brockway, W.J.1    Castellino, F.J.2
  • 4
    • 0014409422 scopus 로고
    • Interaction of streptokinase and human plasminogen V. Studies on the nature and mechanism of formation of the enzymatic site of the activator complex
    • Buck FF, Hummel BCW, De Renzo EC. 1968. Interaction of streptokinase and human plasminogen V. Studies on the nature and mechanism of formation of the enzymatic site of the activator complex. J Biol Chem 243:3648-3654.
    • (1968) J Biol Chem , vol.243 , pp. 3648-3654
    • Buck, F.F.1    Hummel, B.C.W.2    De Renzo, E.C.3
  • 6
    • 0023006174 scopus 로고
    • Regulation of the streptokinase-mediated activation of human plasminogen by fibrinogen and chloride ions
    • Chibber BAK, Castellino FJ. 1986. Regulation of the streptokinase-mediated activation of human plasminogen by fibrinogen and chloride ions. J Biol Chem 261:5289-5295.
    • (1986) J Biol Chem , vol.261 , pp. 5289-5295
    • Chibber, B.A.K.1    Castellino, F.J.2
  • 7
    • 85016899258 scopus 로고
    • Streptococcal fibrinolysis: A proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin
    • Christensen LR. 1945. Streptococcal fibrinolysis: A proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin. J Gen Physiol 28:363-383.
    • (1945) J Gen Physiol , vol.28 , pp. 363-383
    • Christensen, L.R.1
  • 9
    • 0025219617 scopus 로고
    • Plasminogen activator activities of equimolar complexes of streptokinase with variant recombinant plasminogens
    • Davidson DJ, Higgins DL, Castellino FJ. 1990. Plasminogen activator activities of equimolar complexes of streptokinase with variant recombinant plasminogens. Biochemistry 29:3585-3590.
    • (1990) Biochemistry , vol.29 , pp. 3585-3590
    • Davidson, D.J.1    Higgins, D.L.2    Castellino, F.J.3
  • 10
    • 0028075741 scopus 로고
    • Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase
    • Dawson KM, Marshall JM, Raper RH, Gilbert RJ, Ponting CP. 1994. Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase. Biochemistry 33:12042-12047.
    • (1994) Biochemistry , vol.33 , pp. 12042-12047
    • Dawson, K.M.1    Marshall, J.M.2    Raper, R.H.3    Gilbert, R.J.4    Ponting, C.P.5
  • 11
    • 0026654913 scopus 로고
    • Secondary structure of streptokinase in aqueous solution: A Fourier transform infrared spectroscopic study
    • Fabian H, Naumann D, Misselwitz R, Ristau O, Gerlach D, Welfle H. 1992. Secondary structure of streptokinase in aqueous solution: A Fourier transform infrared spectroscopic study. Biochemistry 31.6532-6538.
    • (1992) Biochemistry , vol.31 , pp. 6532-6538
    • Fabian, H.1    Naumann, D.2    Misselwitz, R.3    Ristau, O.4    Gerlach, D.5    Welfle, H.6
  • 12
    • 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 41,299 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 41,299 cases of suspected acute myocardial infarction. Lancet 339:753-781.
    • (1992) Lancet , vol.339 , pp. 753-781
  • 13
    • 0022535440 scopus 로고
    • Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues
    • Jackson KW, Malke H, Gerlach D, Ferretti JJ, Tang J. 1986. Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues. Biochemistry 25:108-114.
    • (1986) Biochemistry , vol.25 , pp. 108-114
    • Jackson, K.W.1    Malke, H.2    Gerlach, D.3    Ferretti, J.J.4    Tang, J.5
  • 14
    • 0020306559 scopus 로고
    • Complete amino acid sequence of streptokinase and its homology with serine proteases
    • Jackson KW, Tang J. 1982. Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry 21:6620-6625.
    • (1982) Biochemistry , vol.21 , pp. 6620-6625
    • Jackson, K.W.1    Tang, J.2
  • 15
    • 0016679019 scopus 로고
    • The activation by staphylokinase of human plasminogen
    • Kowalska-Loth B, Zakrzewski K. 1975. The activation by staphylokinase of human plasminogen. Acta Biochim Pol 22:327-339.
    • (1975) Acta Biochim Pol , vol.22 , pp. 327-339
    • Kowalska-Loth, B.1    Zakrzewski, K.2
  • 16
    • 0027982294 scopus 로고
    • Characterization of the interaction between plasminogen and staphylokinase
    • Lijnen HR, De Cock F, Van Hoef B, Schlott B, Collen D. 1994. Characterization of the interaction between plasminogen and staphylokinase. Eur J Biochem 224:143-149.
    • (1994) Eur J Biochem , vol.224 , pp. 143-149
    • Lijnen, H.R.1    De Cock, F.2    Van Hoef, B.3    Schlott, B.4    Collen, D.5
  • 17
    • 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 43:694-702.
    • (1971) Biochem Biophys Res Commun , vol.43 , pp. 694-702
    • McClintock, D.K.1    Bell, P.H.2
  • 18
    • 0002550822 scopus 로고
    • Streptokinase. Expression of altered forms
    • Washington DC: American Society for Microbiology
    • Malke H, Lorenz D, Ferretti JJ. 1987. Streptokinase. Expression of altered forms. In: Streptococcal genetics. Washington DC: American Society for Microbiology. pp 143-149.
    • (1987) Streptococcal Genetics , pp. 143-149
    • Malke, H.1    Lorenz, D.2    Ferretti, J.J.3
  • 19
    • 0021885514 scopus 로고
    • Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A
    • Malke H, Roe B, Ferretti JJ. 1985. Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene 34:357-362.
    • (1985) Gene , vol.34 , pp. 357-362
    • Malke, H.1    Roe, B.2    Ferretti, J.J.3
  • 20
    • 0017098864 scopus 로고
    • Activator activities of the transient forms of the human plasminogen-streptokinase complex during its proteolytic conversion to the stable activator complex
    • Markus G, Evers JL, Hobika GH. 1976. Activator activities of the transient forms of the human plasminogen-streptokinase complex during its proteolytic conversion to the stable activator complex. J Biol Chem 251: 6495-6504.
    • (1976) J Biol Chem , vol.251 , pp. 6495-6504
    • Markus, G.1    Evers, J.L.2    Hobika, G.H.3
  • 21
    • 0022454070 scopus 로고
    • Identification of t-PA as the major active plasminogen activator in human milk
    • Marshall JM, Rees MCP, Cederholm-Williams SA. 1986. Identification of t-PA as the major active plasminogen activator in human milk. Thromb Haem 55:279-281.
    • (1986) Thromb Haem , vol.55 , pp. 279-281
    • Marshall, J.M.1    Rees, M.C.P.2    Cederholm-Williams, S.A.3
  • 24
    • 0025475363 scopus 로고
    • Fibrin-dependent activation of plasminogen by a proteolytic digest of streptokinase
    • Nakashima A, Okada T, Sugie I. 1990. Fibrin-dependent activation of plasminogen by a proteolytic digest of streptokinase. Fibrinolysis 1:279-284.
    • (1990) Fibrinolysis , vol.1 , pp. 279-284
    • Nakashima, A.1    Okada, T.2    Sugie, I.3
  • 25
    • 0028203899 scopus 로고
    • Unfolding studies of the protease domain of urokinase-type plasminogen activator: The existence of partly folded states and stable subdomains
    • Nowak UK, Cooper A, Saunders D, Smith RAG, Dobson CM. 1994. Unfolding studies of the protease domain of urokinase-type plasminogen activator: The existence of partly folded states and stable subdomains. Biochemistry 33:2951-2960.
    • (1994) Biochemistry , vol.33 , pp. 2951-2960
    • Nowak, U.K.1    Cooper, A.2    Saunders, D.3    Smith, R.A.G.4    Dobson, C.M.5
  • 26
    • 0027354759 scopus 로고
    • Direct quantitative determination of peptides and proteins in PVDF transfer membrane using a computing densitometer
    • Parrado J, Ayala A, Machado A. 1993. Direct quantitative determination of peptides and proteins in PVDF transfer membrane using a computing densitometer. Peptide Res 6:13-16.
    • (1993) Peptide Res , vol.6 , pp. 13-16
    • Parrado, J.1    Ayala, A.2    Machado, A.3
  • 28
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel A, Park K, Fasman GD. 1992. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide. Anal Biochem 203:83-93.
    • (1992) Anal Biochem , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 29
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins SJ. 1986. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur J Biochem 157:169-180.
    • (1986) Eur J Biochem , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 30
    • 0024382525 scopus 로고
    • Conformational properties of streptokinase
    • Radek JT, Castellino FJ. 1989. Conformational properties of streptokinase. J Biol Chem 264:9915-9922.
    • (1989) J Biol Chem , vol.264 , pp. 9915-9922
    • Radek, J.T.1    Castellino, F.J.2
  • 31
    • 0016250250 scopus 로고
    • Esterase activities in the zymogen moiety of the streptokinase-plasminogen complex
    • Reddy KNN, Markus G. 1974. Esterase activities in the zymogen moiety of the streptokinase-plasminogen complex. J Biol Chem 249:4851-4857.
    • (1974) J Biol Chem , vol.249 , pp. 4851-4857
    • Reddy, K.N.N.1    Markus, G.2
  • 32
    • 0029079778 scopus 로고
    • Identification of a plasminogen binding region in streptokinase that is necessary for the creation of r 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 r functional streptokinase-plasminogen activator complex. Biochemistry 34:10266-10211.
    • (1995) Biochemistry , vol.34 , pp. 10266-110211
    • Reed, G.L.1    Lin, L.F.2    Parhami-Seren, B.3    Kussie, P.4
  • 35
    • 0023472472 scopus 로고
    • Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa
    • Shägger H, Von Jagow G. 1987. Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Shägger, H.1    Von Jagow, G.2
  • 36
    • 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
  • 37
    • 0017126765 scopus 로고
    • Interaction of streptokinase with plasminogen. Isolation and characterization of a streptokinase degradation product
    • Siefring GE, Castellino FJ. 1976. Interaction of streptokinase with plasminogen. Isolation and characterization of a streptokinase degradation product. J Biol Chem 251:3913-3920.
    • (1976) J Biol Chem , vol.251 , pp. 3913-3920
    • Siefring, G.E.1    Castellino, F.J.2
  • 38
    • 0019864396 scopus 로고
    • Fibrinolysis with acyl enzymes - A new approach to thrombolytic therapy
    • Smith RAG, Dupe RJ, English PD, Green J. 1981. Fibrinolysis with acyl enzymes - A new approach to thrombolytic therapy. Nature 290:505-508.
    • (1981) Nature , vol.290 , pp. 505-508
    • Smith, R.A.G.1    Dupe, R.J.2    English, P.D.3    Green, J.4
  • 39
    • 0016230594 scopus 로고
    • The interaction of streptokinase with human, cat, dog, and rabbit plasminogens. The fragmentation of streptokinase in the equimolar plasminogen-streptokinase complexes
    • Summaria L, Arzadon L, Bernabe P, Robbins KC. 1974. The interaction of streptokinase with human, cat, dog, and rabbit plasminogens. The fragmentation of streptokinase in the equimolar plasminogen-streptokinase complexes. J Biol Chem 249:4760-4769.
    • (1974) J Biol Chem , vol.249 , pp. 4760-4769
    • Summaria, L.1    Arzadon, L.2    Bernabe, P.3    Robbins, K.C.4
  • 40
    • 0017171808 scopus 로고
    • Isolation of a human plasmin-derived, functionally active, light(B) chain capable of forming with streptokinase an equimolar light(B) chain-streptokinase complex with plasminogen activator activity
    • Summaria L, Robbins KC. 1976. Isolation of a human plasmin-derived, functionally active, light(B) chain capable of forming with streptokinase an equimolar light(B) chain-streptokinase complex with plasminogen activator activity. J Biol Chem 251:5810-5813.
    • (1976) J Biol Chem , vol.251 , pp. 5810-5813
    • Summaria, L.1    Robbins, K.C.2
  • 41
    • 0027408179 scopus 로고
    • Characterization of structural and folding properties of streptokinase by N.M.R. spectroscopy
    • Teuten AJ, Broadhurst RW, Smith RAG, Dobson CM. 1993. Characterization of structural and folding properties of streptokinase by N.M.R. spectroscopy. Biochem J 90:313-319.
    • (1993) Biochem J , vol.90 , pp. 313-319
    • Teuten, A.J.1    Broadhurst, R.W.2    Smith, R.A.G.3    Dobson, C.M.4
  • 43
    • 0018873898 scopus 로고
    • 2-antiplasmin
    • 2-antiplasmin. Thromb Res 17:143-152.
    • (1980) Thromb Res , vol.17 , pp. 143-152
    • Wiman, B.1
  • 44
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.