Photoaffinity labeling of an acorn barnacle lectin with a photoactivatable fluorescent reagent derivative of d-galactosamine

Koji Muramoto, Hisao Kamiya

    Research output: Contribution to journalArticlepeer-review

    7 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)1-8
    Number of pages8
    JournalDevelopmental and Comparative Immunology
    Volume16
    Issue number1
    DOIs
    Publication statusPublished - 1992 Jan 1

    Keywords

    • Amino acid sequence
    • Carbohydrate binding site
    • Lectin
    • Megabalanus rosa
    • Photoaffinity labeling
    • acorn barnacle
    • invertebrate lectin

    ASJC Scopus subject areas

    • Immunology
    • Developmental Biology

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