Abstract
Monoclonal antibodies directed against a 32-kilodalton (kDa) protein of Mycoplasma pneumoniae have been used to characterize a hemadsorption-negative (HA-) mutant class whose protein profile was previously indistinguishable from the wild-type, hemadsorbing (HA+) strain. Electron microscopy and colloidal gold labeling techniques were applied for ultrastructural analysis of the 32-kDa protein. Results indicate that this protein clusters in the tip structure of M. pneumoniae (HA+) wild-type organisms. Additionally, the protein is precipitated by infected hamster sera.
Original language | English (US) |
---|---|
Pages (from-to) | 474-479 |
Number of pages | 6 |
Journal | Israel journal of medical sciences |
Volume | 23 |
Issue number | 5 |
State | Published - May 1987 |
ASJC Scopus subject areas
- Bioengineering