Purification and properties of a binding protein for branched-chain amino acids in Pseudomonas aeruginosa.
A binding protein for branched-chain amino acids was purified to a homogeneous state from shock fluid of Pseudomonas aeruginosa PML14. It was a monomeric protein with an apparent molecular weight of 4.3 x 10(4) or 4.0 x 10(4) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis or gel filtra...
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| Udgivet i: | J Bacteriol |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Microbiology (ASM)
1980
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC293780/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6767701/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.141.3.1055-1063.1980 |
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