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
Externally publishedYes

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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