1. Penicillin-binding proteins in Borrelia burgdorferi
- Author
-
Peter D. Gorevic, R J Dattwyller, B J Luft, J J Rahal, and Carl Urban
- Subjects
Protein Denaturation ,Penicillin binding proteins ,Penicillins ,Spirochaetaceae ,Muramoylpentapeptide Carboxypeptidase ,Microbiology ,DNA-binding protein ,Bacterial Proteins ,Borrelia burgdorferi Group ,polycyclic compounds ,medicine ,Penicillin-Binding Proteins ,Borrelia burgdorferi ,Molecular Biology ,Gel electrophoresis ,biology ,biology.organism_classification ,Molecular biology ,Molecular Weight ,Penicillin ,Membrane ,Hexosyltransferases ,Biochemistry ,Peptidyl Transferases ,Electrophoresis, Polyacrylamide Gel ,Carrier Proteins ,Bacteria ,Research Article ,medicine.drug - Abstract
Penicillin-binding proteins were identified in Borrelia burgdorferi membranes. A 94-kilodalton penicillin-binding protein was the first to be labeled with tritiated penicillin and was the first band to disappear in a competition experiment. Its binding ability was destroyed when membranes were preboiled. In addition, several of these penicillin-binding proteins comigrated with bands previously identified as surface proteins.
- Published
- 1990