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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...

Täydet tiedot

Tallennettuna:
Julkaisussa:Infect Immun
Päätekijät: Fehniger, T E, Walfield, A M, Cunningham, T M, Radolf, J D, Miller, J N, Lovett, M A
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Microbiology (ASM) 1984
Aiheet:
Research Article
Linkit: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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