Aspartokinase of Streptococcus mutans: purification, properties, and regulation.
Aspartokinase from Streptococcus mutans BHT was purified to homogeneity and characterized. The molecular weight of the native enzyme was estimated to be 242,000 by gel filtration. Cross-linking of aspartokinase with dimethyl suberimidate and polyacrylamide gel electrophoresis of the amidinated enzym...
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| Udgivet i: | J Bacteriol |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Microbiology (ASM)
1978
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC222277/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/26656/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.134.2.483-491.1978 |
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