ABSTRACT
A mitogenic lectin for human lymphocytes is present in the marine sponge Desmapsama anchorata. The protein hemagglutinates red blood cells irrespective of ABO group antigens. We now report the isolation of this lectin, by affinity chromatography on a column of raffinose conjugated to epoxy-activated Sepharose 6B, in 8.3% yield and with a purification index of 27 based on hemagglutinating activity. The isolated lectin is a glycoprotein with two subunits with molecular weights of about 18 and 36 kDa which display carbohydrate combining sites of similar specificities and can be associated in different forms
Subject(s)
Chromatography, Affinity , Lectins/isolation & purification , Porifera/analysis , Electrophoresis, Polyacrylamide Gel , HemagglutinationABSTRACT
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 ther 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 periheral 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