Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance

Protein Science

Volumn 5, Issue 12, 1996, Pages 2583-2591

  Conejero Lara, Francisco ^a,d   Parrado, Juan ^a   Azuaga, Ana I ^a,d   Smith, Richard A G ^b   Ponting, Christopher P ^c   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b GLAXOSMITHKLINE   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF GRANADA   (Spain)

Author keywords

circular dichroism; domains; fibrinolysis; NMR; protein fragments; streptokinase; thermal stability

Indexed keywords

STREPTOKINASE;

ARTICLE; CIRCULAR DICHROISM; FIBRINOLYSIS; HEART INFARCTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STOICHIOMETRY; THERMOSTABILITY;

STREPTOCOCCUS; STREPTOCOCCUS DYSGALACTIAE SUBSP. EQUISIMILIS;

EID: 0030448926     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051221     Document Type: Article

References (34)

1. Bakker AHF, Weening-Verhoeff EJD, Verheijen JH. 1995 The role of the lysyl binding site of tissue-type plasminogen activator in the interaction with a forming fibrin clot. J Biol Chem 270.12355-12360.
2. Brandts JF, Hu CQ, Lin LN, Mas MT. 1989. A simple model for proteins with interacting domains. Applications to scanning calorimetry data. Biochemistry 28:8588-8596
3. Brockway WJ, Castellino FJ. 1974. A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex. Biochemistry 13:2063-2070.
4. Damaschun G, Damaschun H, Gast K, Gerlach D, Misselwitz R, Welfle H, Zirwer D. 1992. Streptokinase is a flexible multi-domain protein. Eur Biophys J 20:355-361.
5. De Laureto PP, De Filippis V, Scaramella E, Zambonin M, Fontana A. 1995 Limited proteolysis of lysozyme in trifluoroethanol - Isolation and characterization of a partially active enzyme derivative. Eur J Biochem 230:779-787.
6. De Prat Gay G, Fersht AR. 1994. Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue. Biochemistry 33.7957-7963.
7. Freire E, Murphy KP, Sanchez-Ruiz JM, Galisteo ML, Privalov PL. 1992. The molecular basis of cooperatively in protein folding Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase. Biochemistry 31:250-256.
8. 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. Lancer 339:753-781.
9. 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.
10. Kurochkin IV, Procyk R, Bishop PD, Yee VC, Teller DC, Ingham KC, Medved LV. 1995. Domain structure, stability and domain-domain interactions in recombinant factor XIII. J Mol Biol 248:414-430.
11. Malke H, Lorenz D, Ferretti J. 1987. Streptokinase: Expression of altered forms. In: Ferretti JJ and Curtiss R III, eds. Streptococcal genetics. Washington DC: American Society for Microbiology. pp 143-149.
12. Marshall JM, Brown AJ, Ponting CP. 1994. Conformational studies of human plasminogen fragments: Evidence for a novel third conformation of plasminogen. Biochemistry 33:3599-3606.
13. Martin M. 1982. Streptokinase in chronic arterial diseases. Boca Raton, FL: CRC Press, Inc.
14. McClintock DK, Bell PH. 1971. The mechanism of activation of human plasminogen by streptokinase. Biochem Biophys Res Commun 43:694-702.
15. Misselwitz R, Kraft R, Kostka S, Fabian H, Welfle K, Pfeil W, Welfle H, Gerlach D. 1992. Limited proteolysis of streptokinase and properties of some fragments. In: J Biol Macromol 14:107-116.
16. Novokhatny VV, Ingham KC, Medved LV. 1991. Domain structure and domain-domain interactions of recombinant tissue plasminogen activator. J Biol Chem 260:12994-13002.
17. 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.
18. 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
19. Pautov VD, Anufrieva EV, Ananéva, TD, Saveléva NV, Taratina TM, Krakovyak MG. 1990. Structural-dynamic and functional properties of native and modified streptokinase. Molecular Biology (Trans Molek Biol) 24:35-41.
20. Privalov PL. 1979. Stability of proteins: Small globular proteins. Adv Prot Chem 33:167-241.
21. Radek JT, Castellino FJ. 1989. Conformational properties of streptokinase. J Biol Chem 264:9915-9922.
22. 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.
23. Rodríguez P, Fuentes D, Muñoz E, Rivero D, Orta D, Alburquerque S, Perez S, Besada V, Herrera L. 1994. The streptokinase domain responsible for plasminogen binding. Fibrinolysis 8:276-285.
24. Rodríguez P, Fuentes P, Barro M, Alvarez JG, Muñoz E, Collen D, Lijnen R. 1995. Structural domains of streptokinase involved in the interaction with plasminogen. Eur J Biochem 229:83-90.
25. 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.
26. Shi GY, Chang BI, Chen SM, Wu DH, Wu HL. 1994 Function of streptokinase fragments in plasminogen activation. Biochem J 304:235-241.
27. Siefring GE, Castellino FJ. 1976. Interaction of streptokinase with plasminogen. Isolation and characterization of a streptokinase degradation product J Biol Chem 251:3913-3920.
28. Sun AQ, Yuksel KU, Gracy RW. 1993. Limited proteolysis of tnose-phosphate isomerase and characterization of the catalytically active peptide complex. J Biol Chem 268:26872-26878.
29. Tasayco ML, Chao K. 1995. NMR-study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation. Proteins Struct Funct Genet 22:41-44.
30. Teuten AJ, Broadhurst RW, Smith RAG, Dobson CM. 1993. Characterization of structural and folding properties of streptokinase by n m.r spectroscopy. Biochem J 290:313-319.
31. Teuten AJ, Smith RAG, Dobson CM. 1991. Domain interactions in human plasminogen studied by proton NMR. FEBS Lett 275:17-22.
32. Vysotchin A, Medved LV, Ingham KC. 1993. Domain structure and domain-domain interactions in human coagulation factor IX. J Biol Chem 268:8436-8446
33. Welfle H, Misselwitz R, Fabian H, Damerau W, Hoelzer W, Gerlach D, Kalnin NN, Venyaminov SY. 1992. Conformational properties of streptokinase - Secondary structure and localization of aromatic amino acids. Int J Biol Macromol 14:9-22.
34. Young KC, Shi GY, Chang YF, Chang BI, Chang LC, Lai MD, Chuang WJ, Wu HL. 1995. Interaction of streptokinase and plasminogen studied with truncated streptokinase peptides. J Biol Chem 270:29601-29606.