Work

Five Penicillin-binding Components Occur in Bacillus subtilis Membranes

Year: 1972

Type: article

Abstract: Membranes of Bacillus subtilis to which [14C]penicillin G had been bound were fractionated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Five labeled components were separated. These five components differed from each other in the rates at which they bound penicillins and cephalosporins by up to four orders of magnitude. The major penicillin-binding component, V, was identified as the d-alanine carboxypeptidase, whose activity is not vital for the cell. Three of the other components, in contrast, bound penicillins and cephalosporins at rates comparable to that of the penicillin killing site in this organism.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(20)81815-8

Authors: Peter M. Blumberg, Jack L. Strominger

Institution: Harvard University

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1530645968

FWCI: 5.471

Cites: 32

Cited by: 96

Related to: 10