A lipopolysaccharide-binding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs.
Campylobacter fetus cells can produce multiple S-layer proteins ranging from 97 to 149 kDa, with a single form predominating in cultured cells. We have cloned, sequenced, and expressed in Escherichia coli a sapA homolog, sapA2, which encodes a full-length 1,109-amino-acid (112-kDa) S-layer protein....
Sparad:
| I publikationen: | J Bacteriol |
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| Huvudupphov: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Utgiven: |
American Society for Microbiology (ASM)
1995
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC176800/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7896695/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.177.7.1734-1741.1995 |
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