Gerlach D - Search Results

1

Conformational properties of streptokinase--differential scanning calorimetric investigations.

Welfle K, Pfeil W, Misselwitz R, Welfle H, Gerlach D. Welfle K, et al. Among authors: gerlach d. Int J Biol Macromol. 1992 Feb;14(1):19-22. doi: 10.1016/s0141-8130(05)80014-5. Int J Biol Macromol. 1992. PMID: 1596467

2

Conformational properties of streptokinase--secondary structure and localization of aromatic amino acids.

Welfle H, Misselwitz R, Fabian H, Damerau W, Hoelzer W, Gerlach D, Kalnin NN, Venyaminov SY. Welfle H, et al. Among authors: gerlach d. Int J Biol Macromol. 1992 Feb;14(1):9-18. doi: 10.1016/s0141-8130(05)80013-3. Int J Biol Macromol. 1992. PMID: 1317718

3

Limited proteolysis of streptokinase and properties of some fragments.

Misselwitz R, Kraft R, Kostka S, Fabian H, Welfle K, Pfeil W, Welfle H, Gerlach D. Misselwitz R, et al. Among authors: gerlach d. Int J Biol Macromol. 1992 Apr;14(2):107-16. doi: 10.1016/0141-8130(92)90007-u. Int J Biol Macromol. 1992. PMID: 1515400

4

Streptokinase is a flexible multi-domain protein.

Damaschun G, Damaschun H, Gast K, Gerlach D, Misselwitz R, Welfle H, Zirwer D. Damaschun G, et al. Among authors: gerlach d. Eur Biophys J. 1992;20(6):355-61. doi: 10.1007/BF00196594. Eur Biophys J. 1992. PMID: 1313757

5

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. Fabian H, et al. Among authors: gerlach d. Biochemistry. 1992 Jul 21;31(28):6532-8. doi: 10.1021/bi00143a024. Biochemistry. 1992. PMID: 1633164

6

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

Welfle K, Misselwitz R, Schaup A, Gerlach D, Welfle H. Welfle K, et al. Among authors: gerlach d. Proteins. 1997 Jan;27(1):26-35. Proteins. 1997. PMID: 9037709

7

Inactivation of the streptokinase gene prevents Streptococcus equisimilis H46A from acquiring cell-associated plasmin activity in the presence of plasminogen.

Malke H, Mechold U, Gase K, Gerlach D. Malke H, et al. Among authors: gerlach d. FEMS Microbiol Lett. 1994 Feb 1;116(1):107-12. doi: 10.1111/j.1574-6968.1994.tb06683.x. FEMS Microbiol Lett. 1994. PMID: 8132150

8

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. Jackson KW, et al. Among authors: gerlach d. Biochemistry. 1986 Jan 14;25(1):108-14. doi: 10.1021/bi00349a016. Biochemistry. 1986. PMID: 3954985

The streptokinase expressed by the cloned gene in Streptococcus sanguis has a molecular weight of about 44 000 [Malke, H., Gerlach, D., Kohler, W., & Ferretti, J.J. (1984) MGG, Mol. Gen. Genet. 196, 360-365] while the molecular weight of the native streptokinase …

The streptokinase expressed by the cloned gene in Streptococcus sanguis has a molecular weight of about 44 000 [Malke, H., Gerlach, …

9

Purification and characterization of the bacterial plasminogen activator staphylokinase secreted by a recombinant Bacillus subtilis.

Gerlach D, Kraft R, Behnke D. Gerlach D, et al. Zentralbl Bakteriol Mikrobiol Hyg A. 1988 Nov;269(3):314-22. doi: 10.1016/s0176-6724(88)80174-3. Zentralbl Bakteriol Mikrobiol Hyg A. 1988. PMID: 3146168

10

Susceptibility of chicken embryos to group A streptococci: correlation with fibrinogen binding.

Schmidt KH, Wiesner J, Gerlach D, Reichardt W, Ozegowski JH, Köhler W. Schmidt KH, et al. Among authors: gerlach d. FEMS Immunol Med Microbiol. 1993 Oct;7(3):231-40. doi: 10.1111/j.1574-695X.1993.tb00403.x. FEMS Immunol Med Microbiol. 1993. PMID: 8275054

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