Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein.
Copyright policy )Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein.
Penicillin-binding protein 5 of Streptococcus faecium has been solubilized and partially separated from other membrane proteins by covalent affinity chromatography. PBP 5 was successively purified to homogeneity by resolution on SDS-polyacrylamide gel, elution and renaturation of penicillin-binding activity. The purification procedure does not alter the properties that the protein exhibits in the membranous environment.
- University of Verona Italy
Protein Denaturation, Cell Membrane, Streptococcus, Carboxypeptidases, Penicillins, Muramoylpentapeptide Carboxypeptidase, Chromatography, Affinity, Molecular Weight, Bacterial Proteins, Hexosyltransferases, Peptidyl Transferases, Penicillin-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Carrier Proteins
Protein Denaturation, Cell Membrane, Streptococcus, Carboxypeptidases, Penicillins, Muramoylpentapeptide Carboxypeptidase, Chromatography, Affinity, Molecular Weight, Bacterial Proteins, Hexosyltransferases, Peptidyl Transferases, Penicillin-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Carrier Proteins
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