1887

Abstract

Summary: Four of the five penicillin-binding proteins in the cytoplasmic membranes of have been purified to protein homogeneity. The method used involved the solubilization of the penicillin-binding proteins from the membranes by treatment with non-ionic detergent, followed by partial separation of the proteins by ion-exchange chromatography on DEAE-Sepharose CL-6B. Each protein was then purified to protein homogeneity by covalent affinity chromatography on ampicillin–affinose. The protein with the lowest molecular weight is a -carboxypeptidase. The other three proteins have previously been postulated to be peptidoglycan transpeptidases, endopeptidases or -carboxypeptidases , but it was not possible to demonstrate any of these activities with the purified proteins in various systems. Possible reasons for the observed lack of enzymic activity are discussed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-117-1-211
1980-03-01
2019-12-05
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-117-1-211
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error