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

✍ Scribed by K. Welfle; R. Misselwitz; A. Schaup; D. Gerlach; H. Welfle

• Book ID: 101228472
• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 172 KB
• Volume: 27
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199701)27:1<26::aid-prot4>3.0.co;2-l

✦ Synopsis

Conformation and stability of three Sks from Streptococcus equisimilis strain H46A, Streptococcus pyogenes strain A374, and Streptococcus pyogenes strain AT27 were compared by limited proteolysis, CD, and fluorescence measurements and by DSC. The general similarity of the peptide CD spectra in the spectral region 185 to 260 nm indicates the same type of folding for the three proteins. Fluorescence and aromatic CD spectra are consistent with a predominant surface localization of the aromatic amino acids and a low rigidity of their surroundings. A major difference among the three Sks is shown by deconvolution of their excessive heat capacity functions.