Isolation and functional characterization of a mitogenic lectin from the marine sponge Cinachyrella alloclada

Braz J Med Biol Res. 1989;22(3):379-85.

Abstract

1. A D-galactose-specific lectin was isolated from crude extracts of the marine sponge Cinachyrella alloclada by affinity chromatography on Sepharose 4B. 2. The lectin agglutinated human erythrocytes irrespective of their ABO group antigens. 3. Hemagglutination inhibition tests indicated that the lectin binds D-galactose or carbohydrates having a terminal nonreducing D-galactosyl group. 4. C. alloclada lectin was mitogenic for human peripheral blood lymphocytes when AB serum was omitted during the first 24 h of culture. 5. Human serum apparently contains substances which bind or inactivate this lectin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium-Binding Proteins*
  • Carrier Proteins / isolation & purification*
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Erythrocytes / drug effects
  • Hemagglutination
  • Lectins / isolation & purification*
  • Monosaccharide Transport Proteins*
  • Periplasmic Binding Proteins*
  • Porifera / analysis*

Substances

  • Calcium-Binding Proteins
  • Carrier Proteins
  • Lectins
  • Monosaccharide Transport Proteins
  • Periplasmic Binding Proteins
  • galactose-binding protein