Galactose-specific lectin in the hemolymph of solitary ascidian, Halocynthia roretzi. Molecular, binding and functional properties.
Galactose-specific lectin isolated from the hemolymph of solitary ascidian, Halocynthia roretzi, has been further characterized. The hemagglutinating activity of the lectin is Ca2+-dependent. The lectin has a large molecular form as revealed by gel-permeation chromatography, sedimentation equilibrium and velocity measurement, and electron microscopic observation. The lectin is adsorbed to columns of blue-Sepharose and phenyl-Sepharose, and eluted with ethylene glycol, not with lactose or high concentration of NaCl. The lectin shows a stimulatory effect on the superoxide anion production by guinea-pig polymorphonuclear leukocytes, and the effect is inhibited, among various sugars, most strongly by melibiose.
D000818:Animals; D002118:Calcium; D003208:Concanavalin A; D005690:Galactose; D006168:Guinea Pigs; D006384:Hemagglutination; D006458:Hemolymph / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D008854:Microscopy, Electron; D008970:Molecular Weight; D009504:Neutrophils / Q000378:metabolism; D013481:Superoxides / Q000097:blood; D014561:Urochordata / Q000032:analysis*
D037102:Lectins; D003208:Concanavalin A; D013481:Superoxides; D002118:Calcium; D005690:Galactose