A mitogenic lectin in the skin mucus of the kingklip Genypterus capens
is was purified by a combination of affinity adsorption on the glutara
ldehyde-fixed rabbit erythrocyte ghosts and chromatofocusing on PBE 94
gels. The lectin was a glycoprotein having a molecular weight of 28-3
4 kDa which was composed with two homogenous subunit (13.7 kDa). The i
soelectric point was 6.45. Kingklip lectin agglutinated rabbit and hor
se eryttirocytes but not human ABO erythrocytes. The hemagglutinating
activity was calcium ion-dependent and was inhibited effectively by as
ialo-mucin Type I and also by simple sugars such as N-acetyl-D-glucosa
mine. The amino-terminal sequence of the kingklip lectin was identifie
d as -Phe-Ala-His-Leu-Ala-Tyr-Leu-Leu-Arg-Ser-Lys-Ala-.