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.
Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein
FONTANA, Roberta
1986-01-01
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.
File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
