Characterization of the N-acetylmuramic acid L-alanine amidase from Bacillus subtilis.
The N-acetylmuramic acid L-alanine amidase from Bacillus subtilis W-23 has been purified to apparent homogeneity. The enzyme is a monomer of molecular weight 51,000, which binds extremely tightly to homologous cell walls but not to heterologous cell walls, even of the closely related strain B. subti...
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| Published in: | J Bacteriol |
|---|---|
| Main Authors: | , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
American Society for Microbiology (ASM)
1976
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC232987/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/821918/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.127.2.803-811.1976 |
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