Polyclonal antisera have been made against synthetic peptides corresponding to the C-terminal octapeptide and N-terminal nonapeptide of bovine MIP26K. Western blot analysis demonstrated significant binding of the C-terminal antiserum to MIP26K of both normal and cataractous human lens. In contrast, the N-terminal antiserum bound to MIP26K of normal lenses, but failed to bind to MIP26K of 7 out of 10 cataractous lenses studied. These results demonstrate for the first time, a covalent change in MIP26K during human cataractogenesis, and strongly suggest that the location of this change is in the N-terminal region of the polypeptide.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 1986 Mar 28|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology