Characterization of the c-type lectin from the marine sponge (stylissa flexibilis)

Abstract

A lectin from the marine sponge Stylissa flexibilis, designated as SFL, was purified by cold ethanol precipitation followed by ion exchange chromatography on DEAE Sepharose column and Sephacryl S-200 gel filtration. SFL is a dimeric glycoprotein of 32 kDa subunits linked by a disulfide bridge with a molecular mass of 64 kDa by SDS-PAGE and 65 kDa by Sephacryl S-200 gel filtration chromatography. The lectin preferential!v agglutinated enzyme treated human A erythrocytes, whereas it did not agglutinate any type of rabbit, human B and O erythrocytes, irrespective of treatment wilh enzymes.