Photochemical cross-linking of beta-galactoside-binding lectin to polylactosamino-proteoglycan of chick embryonic skin.
beta-Galactoside-binding lectin from chick embryonic skin was coupled with a new photoactivatable, radioactive cross-linking reagent, [35S]N-succinimidyl-3 [(2-nitro-4-azidophenyl)-2-aminoethyldithio] propionate, and was allowed to interact with an insoluble preparation from skin. After UV irradiation, the lectin was specifically cross-linked to a high-molecular-weight substance, which was degraded by endo-beta-galactosidase and pronase. This suggests that the endogenous receptor is polylactosamino-proteoglycan. The interaction between the lectin and polylactosaminoglycan has implications for the role of the lectin in embryonic differentiation.
D000818:Animals; D001386:Azides / Q000494:pharmacology*; D002642:Chick Embryo; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D037161:Galectins; D006388:Hemagglutinins; D011134:Polysaccharides / Q000302:isolation & purification / Q000378:metabolism*; D011509:Proteoglycans / Q000302:isolation & purification / Q000378:metabolism*; D012867:Skin / Q000378:metabolism*; D012995:Solubility; D013462:Sulfur Radioisotopes
D001386:Azides; D003432:Cross-Linking Reagents; D037161:Galectins; D006388:Hemagglutinins; D011134:Polysaccharides; D011509:Proteoglycans; D013462:Sulfur Radioisotopes; C042947:polylactosamino-proteoglycan; C033692:3-((2-nitro-4-azidophenyl)-2-aminoethyldithio)-N-succinimidyl propionate