Conformation and stability of streptokinases from nephritogenic and nonnephritogenic strains of streptococci

Proteins: Structure, Function and Genetics

Volumn 27, Issue 1, 1997, Pages 26-35

  Welfle, K ^a,b   Misselwitz, R ^a,b   Schaup, A ^b   Gerlach, D ^c   Welfle, H ^a,b  

^a HUMBOLDT UNIVERSITY   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^c FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

circular dichroism; differential scanning calorimetry; fluorescence spectroscopy; limited proteolysis; Streptococcus equisimilis; Streptococcus pyogenes; streptokinase variants

Indexed keywords

STREPTOKINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME ISOLATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; STREPTOCOCCUS EQUI; STREPTOCOCCUS PYOGENES; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROLYSIS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SPECIES SPECIFICITY; SPECTROMETRY, FLUORESCENCE; STREPTOCOCCUS; STREPTOKINASE; TRYPSIN;

STREPTOCOCCUS DYSGALACTIAE SUBSP. EQUISIMILIS; STREPTOCOCCUS EQUI; STREPTOCOCCUS PYOGENES;

EID: 0031023530     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199701)27:1<26::AID-PROT4>3.0.CO;2-L     Document Type: Article

References (27)

1. Collen, D., Gold, H.K. New developments in thrombolytic therapy. Adv. Exp. Med. Biol. 281:333-354, 1990.
2. Gerlach, D., Köhler, W. Studies on the heterogeneity of streptokinases of different origin. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. 1 Orig. Reihe A 238: 351-371, 1977.
3. Gerlach, D., Köhler, W. Studies on the heterogeneity of streptokinases. IV. Communication: evidence for isostreptokinases in Streptococcus pyogenes type I. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. 1 Orig. Reihe A 248:446-454, 1980.
4. Dillon, H.C., Wannamaker, L.W. Physical and immunological difference among streptokinases. J. Exp. Med. 121: 351-371, 1965.
5. Johnston, K.H., Zabriskie, J.B. Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A. J. Exp. Med. 163: 697-711, 1986.
6. Weinstein, L. Antigenic dissimilarity of streptokinases. Proc. Soc. Exp. Biol. Med. 83:689-691, 1953.
7. Huang, T.T., Malke, H., Ferretti, J.J. The streptokinase gene of group A streptococci: cloning, expression in Escherichia coli, sequence and analysis. Mol. Microbiol. 3:197-205, 1989.
8. Huang, T.T., Malke, H., Ferretti, J.J. Heterogeneity of the streptokinase gene in group A streptococci. Infect. Immun. 57: 502-506, 1989.
9. Malke, H., Roe, B., Ferretti, J.J. Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene 34: 357-362, 1985.
10. Walter, R., Siegel, M., Malke, H. Nucleotide sequence of the streptokinase gene from a Streptococcus pyogenes type I strain. Nucleic Acids Res. 17:1261, 1989.
11. Walter, R., Siegel, M., Malke, H. Nucleotide sequence of the streptokinase gene from a group G streptococcus. Nucleic Acids Res. 17:1262, 1989.
12. Malke, H. Polymorphism of the streptokinase gene: implications for the pathogenesis of post-streptococcal glomerulonephritis. Int. J. Med. Microbiol., Virol., Parasitol. Infect. Dis. 278:246-257, 1993.
13. Okhuni, H., Tomode, Y., Yoshimura, K., Yamamoto, T., Suzuki, H., Yokomuro, K., Johnston, K.H., Zabriskie, J.B. Detection of nephritis strain-associated streptokinase by monoclonal antibodies. J. Med. Microbiol. 35:60-63, 1991.
14. Okada, K., Katano, T., Kamogashira, R., Zahn, R.J., Morimoto, Y., Kagami, S., Yasumoto, K., Kuhara, T., Kuroda, Y. Streptokinase gene variable region classification in streptococci: lack of correlation with post-streptococcal glomerulonephritis. Clin. Nephrol. 44:8-13, 1995.
15. Welfle, H., Misselwitz, R. Fabian, H., Damerau, W., Hoelzer, W., Gerlach, D., Kalnin, N.N., Venyaminov, S.Yu. Conformational properties of streptokinase: secondary structure and localization of aromatic amino acids. Int. J. Biol. Macromol. 14:9-18, 1992.
16. Fabian, H., Naumann, D., Misselwitz, R., Ristau, O., Gerlach, D., Welfle, H. Secondary structure of streptokinase in aqueous solution: a Fourier transform infrared spectroscopic study. Biochemistry 31:6532-6538, 1992.
17. Welfle, K., Pfeil, W., Misselwitz, R., Welfle, H., Gerlach, D. Conformational properties of streptokinase: differential scanning calorimetric investigations. Int. J. Biol. Macromol. 14:19-22, 1992.
18. Radek, J.T., Castellino, F.J. Conformational properties of streptokinase. J. Biol. Chem. 264:9915-9922, 1989.
19. Damaschun, G., Damaschun, H., Gast, K., Gerlach, D. Misselwitz, R., Welfle, H., Zirwer, D. Streptokinase is a flexible multi-domain protein. Eur. Biophys. J. 20:355-361, 1992.
20. Teuten, A.J., Broadhurst, R.W., Smith, R.A.G., Dobson, C.M. Characterization of structural and folding properties of streptokinase by n.m.r. spectroscopy. Biochem. J. 293: 313-319, 1993.
21. Gerlach, D., Koehler, W. Studies on the heterogeneity of streptokinases of different origin. Zentralbl. Bakteriol. Mikrobiol. Hyg. Abt. 1 Orig. A 238:336-349, 1977.
22. Castellino, F.J., Sodetz, J.M., Brockway, W.J., Siefring G.E., Jr. Streptokinase. Meth. Enzymol. 45:244-257, 1976.
23. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
24. Manavalan, P., Johnson, W.C., Jr. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167: 76-85, 1987.
25. Misselwitz, R., Kraft, R., Kostka, S., Fabian, H., Welfle, K., Pfeil, W., Welfle, H., Gerlach, D. Limited proteolysis of streptokinase and properties of proteolytic fragments. Int. J. Biol. Macromol. 14:107-116, 1992.
26. Jackson, K.W., Malke, H., Gerlach, D., Ferretti, J.J., Tang, J. Active streptokinase from cloned gene in Streptococcus sanguis is without the carboxy-terminal 32 residues. Biochemistry 25:108-114, 1986.
27. Manavalan, P., Johnson, W.C. Jr. Sensitivity of circular dichroism to protein tertiary structure class. Nature 305: 831-832, 1983.