Abstract
A full-length cDNA clone for the 13-14 kDa soluble β-galactoside-binding lectin was isolated from a bovine fibroblast cDNA library. The derived amino acid sequence shows eight differences from a preliminary partial amino acid sequence given previously for the bovine heart lectin. This observation led to a re-examination of the data and correction of the heart lectin protein sequence. Except for a possible polymorphism of the heart lectin at position 67, the fibroblast and heart lectin sequences are considered identical. The epitope recognized by two monoclonal anti-(bovine lectin) antibodies, 36/8 and 9/5, was identified as the tetrapeptide sequence W-G-A/S-E/D by the isolation of several different cDNA clones from a human intestine cDNA library. A similar tetrapeptide is present in all of the soluble β-galactoside-binding animal lectins sequenced thus far. It is also found in myelin basic protein, which we show is antigenically cross-reactive with the lectin. In myelin basic protein the tetrapeptide is a part of the major domain previously shown to be responsible for the induction of experimental allergic encephalomyelitis.
Original language | English (US) |
---|---|
Pages (from-to) | 283-290 |
Number of pages | 8 |
Journal | Biochemical Journal |
Volume | 259 |
Issue number | 1 |
DOIs | |
State | Published - 1989 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology