| Autor: |
Jingushi, Seiya, Mitsuyama, Masao, Moriya, Tetsuhiro, Kawabata, Shunichiro, Iwanaga, Sadaaki, Amako, Kazunobu |
| Zdroj: |
Microbiology and Immunology; September 1987, Vol. 31 Issue: 9 p879-889, 11p |
| Abstrakt: |
The antigenic sites on small thin fimbriae of Serratia marcescensstrain US5 were investigated using immunoelectron microscopy and monoclonal antibodies (MAbs). Negative staining of the fimbriae after treatment with MAbs showed a regularly spaced arrangement of the antibody molecules. When the subunit peptide was subjected to immunoblotting using the MAbs, a single band with a molecular weight of approximately 19kD was evident. This binding of the MAbs to the subunit peptide was completely abrogated after treatment with 2‐mercaptoethanol, thereby suggesting the important role of disulfide linkage in the maintenance of the conformation of the antigenic site reacted with MAbs. Amino acid analysis of the subunit peptide revealed two cysteine residues, and cysteine residues were absent in the N‐terminal portion. |
| Databáze: |
Supplemental Index |
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