Purification and characterization of a cloned protease-resistant Treponema pallidum-specific antigen.
A cloned Treponema pallidum antigen, designated 4D, was purified from Escherichia coli predominantly as a 190-kilodalton (kd) polypeptide, although higher oligomeric forms exist. Extensive proteolysis of 4D created a limit digestion product of 90 kd which retained antigenicity with sera from patient...
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| Vydáno v: | Infect Immun |
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| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1984
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC261577/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6389353/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.46.2.598-607.1984 |
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