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Volumn 52, Issue 2, 2007, Pages 395-402

Refolding, purification, and activation of miniplasminogen and microplasminogen isolated from E. coli inclusion bodies

Author keywords

activation; E. coil expression; Inclusion bodies; Microplasmin; Miniplasmin; Refolding

Indexed keywords

MICROPLASMINOGEN PROTEIN, HUMAN; MINIPLASMINOGEN; PEPTIDE FRAGMENT; PLASMINOGEN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33846407211     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.10.012     Document Type: Article
Times cited : (21)

References (18)
  • 2
    • 0020334286 scopus 로고
    • Fibrinolysis and fibrinogenolysis by Val442-plasmin
    • Ney K.A., and Pizzo S.V. Fibrinolysis and fibrinogenolysis by Val442-plasmin. Biochim. Biophys. Acta 708 (1982) 218-224
    • (1982) Biochim. Biophys. Acta , vol.708 , pp. 218-224
    • Ney, K.A.1    Pizzo, S.V.2
  • 5
    • 0029146292 scopus 로고
    • Structure and function of microplasminogen: II. Determinants of activation by urokinase and by the bacterial activator streptokinase
    • Wang J., and Reich E. Structure and function of microplasminogen: II. Determinants of activation by urokinase and by the bacterial activator streptokinase. Protein Sci. 4 (1995) 1768-1779
    • (1995) Protein Sci. , vol.4 , pp. 1768-1779
    • Wang, J.1    Reich, E.2
  • 6
    • 0842282394 scopus 로고    scopus 로고
    • Thrombolytic potency of acid-stabilized plasmin: superiority over tissue-type plasminogen activator in an in vitro model of catheter-assisted thrombolysis
    • Novokhatny V., Taylor K., and Zimmerman T.P. Thrombolytic potency of acid-stabilized plasmin: superiority over tissue-type plasminogen activator in an in vitro model of catheter-assisted thrombolysis. J. Thromb. Haemost. 1 (2003) 1034-1041
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1034-1041
    • Novokhatny, V.1    Taylor, K.2    Zimmerman, T.P.3
  • 7
    • 0034852601 scopus 로고    scopus 로고
    • Plasmin induces local thrombolysis without causing hemorrhage: a comparison with tissue plasminogen activator in the rabbit
    • Marder V.J., Landskroner K., Novokhatny V., Zimmerman T.P., Kong M., Kanouse J.J., and Jesmok G. Plasmin induces local thrombolysis without causing hemorrhage: a comparison with tissue plasminogen activator in the rabbit. Thromb. Haemostasis 86 (2001) 739-745
    • (2001) Thromb. Haemostasis , vol.86 , pp. 739-745
    • Marder, V.J.1    Landskroner, K.2    Novokhatny, V.3    Zimmerman, T.P.4    Kong, M.5    Kanouse, J.J.6    Jesmok, G.7
  • 9
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Express. Purif. 41 (2005) 207-234
    • (2005) Protein Express. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 10
    • 33846463240 scopus 로고    scopus 로고
    • J.V. Jensen, Process of stabilizing therapeutically useful plasmin solutions. In: US Patent & Trademark Office Patent Application Full Text and Image Database, Patent 3,950,513, Novo Terapeutisk Laboratorium A/S (DK), (1976).
  • 11
    • 0032560642 scopus 로고    scopus 로고
    • Fibrinolysis with des-kringle derivatives of plasmin and its modulation by plasma protease inhibitors
    • Komorowicz E., Kolev K., and Machovich R. Fibrinolysis with des-kringle derivatives of plasmin and its modulation by plasma protease inhibitors. Biochemistry 37 (1998) 9112-9118
    • (1998) Biochemistry , vol.37 , pp. 9112-9118
    • Komorowicz, E.1    Kolev, K.2    Machovich, R.3
  • 12
    • 0030051895 scopus 로고    scopus 로고
    • Quantitative comparison of fibrin degradation with plasmin, miniplasmin, neurophil leukocyte elastase and cathepsin G
    • Kolev K., Komorowicz E., Owen W.G., and Machovich R. Quantitative comparison of fibrin degradation with plasmin, miniplasmin, neurophil leukocyte elastase and cathepsin G. Thromb. Haemostasis 75 (1996) 140-146
    • (1996) Thromb. Haemostasis , vol.75 , pp. 140-146
    • Kolev, K.1    Komorowicz, E.2    Owen, W.G.3    Machovich, R.4
  • 13
    • 0028577559 scopus 로고
    • Heparin modulation of the fibrinolytic activity of plasmin, miniplasmin and neutrophil leukocyte elastase in the presence of plasma protease inhibitors
    • Kolev K., Komorowicz E., and Machovich R. Heparin modulation of the fibrinolytic activity of plasmin, miniplasmin and neutrophil leukocyte elastase in the presence of plasma protease inhibitors. Blood Coagul. Fibrin. 5 (1994) 905-911
    • (1994) Blood Coagul. Fibrin. , vol.5 , pp. 905-911
    • Kolev, K.1    Komorowicz, E.2    Machovich, R.3
  • 14
    • 0018101441 scopus 로고
    • On the kinetics of the reaction between human antiplasmin and plasmin
    • Wiman B., and Collen D. On the kinetics of the reaction between human antiplasmin and plasmin. Eur. J. Biochem. 84 (1978) 573-582
    • (1978) Eur. J. Biochem. , vol.84 , pp. 573-582
    • Wiman, B.1    Collen, D.2
  • 15
    • 0030930671 scopus 로고    scopus 로고
    • Kringle 5 of plasminogen is a novel inhibitor of endothelial cell growth
    • Cao Y., Chen A., An S.S., Ji R.W., Davidson D., and Llinas M. Kringle 5 of plasminogen is a novel inhibitor of endothelial cell growth. J. Biol. Chem. 272 (1997) 22924-22928
    • (1997) J. Biol. Chem. , vol.272 , pp. 22924-22928
    • Cao, Y.1    Chen, A.2    An, S.S.3    Ji, R.W.4    Davidson, D.5    Llinas, M.6
  • 16
    • 17644416463 scopus 로고    scopus 로고
    • High level expression of kringle 5 fragment of plasminogen in Pichia pastoris
    • Zhou Y., Zheng Q., Gao J., and Gu J. High level expression of kringle 5 fragment of plasminogen in Pichia pastoris. Biotechnol. Lett. 27 (2005) 167-171
    • (2005) Biotechnol. Lett. , vol.27 , pp. 167-171
    • Zhou, Y.1    Zheng, Q.2    Gao, J.3    Gu, J.4
  • 17
    • 0029664904 scopus 로고    scopus 로고
    • Reaction of human alpha2-antiplasmin and plasmin stopped-flow fluorescence kinetics
    • Christensen U., Bangert K., and Thorsen S. Reaction of human alpha2-antiplasmin and plasmin stopped-flow fluorescence kinetics. FEBS Lett. 387 (1996) 58-62
    • (1996) FEBS Lett. , vol.387 , pp. 58-62
    • Christensen, U.1    Bangert, K.2    Thorsen, S.3
  • 18
    • 0034534977 scopus 로고    scopus 로고
    • Mutational analysis of affinity and selectivity of kringle-tetranectin interaction. Grafting novel kringle affinity onto the tetranectin lectin scaffold
    • Graversen J.H., Jacobsen C., Sigurskjold B.W., Lorentsen R.H., Moestrup S.K., Thogersen H.C., and Etzerodt M. Mutational analysis of affinity and selectivity of kringle-tetranectin interaction. Grafting novel kringle affinity onto the tetranectin lectin scaffold. J. Biol. Chem. 275 (2000) 37390-37396
    • (2000) J. Biol. Chem. , vol.275 , pp. 37390-37396
    • Graversen, J.H.1    Jacobsen, C.2    Sigurskjold, B.W.3    Lorentsen, R.H.4    Moestrup, S.K.5    Thogersen, H.C.6    Etzerodt, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.