title: Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein.
abstract: 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.
mesh_terms: D001426:Bacterial Proteins; D002268:Carboxypeptidases / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006602:Hexosyltransferases; D008970:Molecular Weight; D002267:Muramoylpentapeptide Carboxypeptidase / Q000302:isolation & purification* / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism; D010458:Peptidyl Transferases; D011489:Protein Denaturation; D013291:Streptococcus / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase