1996 Volume 62 Issue 1 Pages 138-141
A mitogenic lectin in the skin mucus of the kingklip Genypterus capensis was purified by a combination of affinity adsorption on the glutaraldehyde-fixed rabbit erythrocyte ghosts and chromatofocusing on PBE 94 gels. The lectin was a glycoprotein having a molecular weight of 28-34 kDa which was composed with two homogenous subunit(13.7 kDa). The isoelectric point was 6.45. Kingklip lectin agglutinated rabbit and horse eryttirocytes but not human ABO erythrocytes. The hemagglutinating activity was calcium ion-dependent and was inhibited effectively by asialo-mucin Type I and also by simple sugars such as N-acetyl-D-glucosamine.The amino-terminal sequence of the kingklip lectin was identified as Ser-Met-Cys-Asn-Cys-Gly-Trp-Ser-Gln-Phe-Ala-His-Leu-Ala-Tyr-Leu-Leu-Arg-Ser-Lys-Ala-.