Isolation by Covalent Affinity Chromatography of the Penicillin-Binding Components from Membranes of Bacillus subtilis
AUTOR(ES)
Blumberg, Peter M.
RESUMO
An affinity chromatography technique was developed to isolate the five penicillin-binding components present in Bacillus subtilis membranes. The proteins were solubilized by the detergent Nonidet P-40, bound covalently to penicillin-substituted Sepharose, and subsequently eluted from the matrix with neutral hydroxylamine, which cleaves the penicilloyl-enzyme bond. Penicillin binding-component V, the D-alanine carboxypeptidase, makes up 1% of the total membrane protein. A modification of the above procedure enabled this enzyme to be obtained from the membrane in pure form in a single step with 50% overall recovery of enzymatic activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389864Documentos Relacionados
- Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis.
- Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
- Penicillin-binding proteins in Bacillus subtilis mutants.
- Changes in penicillin-binding proteins during sporulation of Bacillus subtilis.
- Septal Localization of Penicillin-Binding Protein 1 in Bacillus subtilis
