Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes. [electronic resource]
Producer: 20021126Description: 4839-51 p. digitalISSN:- 0014-2956
- 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
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Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
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