Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes. [electronic resource]
- European journal of biochemistry Oct 2002
- 4839-51 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0014-2956
10.1046/j.1432-1033.2002.03183.x doi
Adhesins, Bacterial Amino Acid Sequence Base Sequence Binding Sites Circular Dichroism DNA, Bacterial--genetics Endopeptidases--chemistry Enzyme Precursors--chemistry Enzyme Stability Escherichia coli--genetics Hot Temperature Humans Hydrolysis In Vitro Techniques Kinetics Molecular Sequence Data Peptide Fragments--chemistry Protein Denaturation Protein Processing, Post-Translational Recombinant Proteins--chemistry Spectrometry, Fluorescence Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Streptococcus pyogenes--enzymology Substrate Specificity