| Literature DB >> 3951364 |
A Grossato, Y R Cheng, E Tonin, P Jacques, R Fontana.
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.Entities:
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Year: 1986 PMID: 3951364
Source DB: PubMed Journal: Microbiologica ISSN: 0391-5352