Abstract
A photoactivatable d-galactosamine derivative was prepared by reaction of the amino group of d-galactosamine with 1-azide-5-naphthalene sulfonyl chloride (ANS-Cl). The derivative (GalN-ANS) inhibited the agglutination activity of an acorn barnacle lectin against rabbit erythrocytes to the same extent as d-galactosamine. We used GalN-ANS for photoaffinity labeling of the lectin. The photolabeled lectin was digested with pronase and the digest was separated by reversed-phase high-performance liquid chromatography by monitoring fluorescence and uv absorption to isolate the peptide labeled with GalN-ANS. Amino acid analyses of the labeled peptides revealed that GalN-ANS preferentially covalently labeled two regions in the carbohydrate recognition domain of the lectin. One of them was the highly conserved amino-acid sequence region throughout all calcium-dependent animal lectins.
| Original language | English |
|---|---|
| Pages (from-to) | 1-8 |
| Number of pages | 8 |
| Journal | Developmental and Comparative Immunology |
| Volume | 16 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1992 |
| Externally published | Yes |
Keywords
- Amino acid sequence
- Carbohydrate binding site
- Lectin
- Megabalanus rosa
- Photoaffinity labeling
- acorn barnacle
- invertebrate lectin
ASJC Scopus subject areas
- Immunology
- Developmental Biology