A new agglutinating activity from wheat flour inhibited by tryptophan.
A new compound endowed with agglutinating activity, designated the flour agglutinin, was extracted from wheat flour with water and purified by gel filtration and ion-exchange chromatography. The haptenic inhibitors of the plant agglutinins do not affect flour agglutinin activity which, on the other hand, is inhibited by D- and L-tryptophan. Flour agglutinin has a molecular weight of about 5 - 10(4) as determined by gel filtration. It consists of a neutral heteropolysaccharide constituted of D-xylose and L-arabinose, and is homogeneous as judged by sedimentation analysis. Flour agglutinin activity is destroyed by treatment with Cellulase 2000 and periodate, but is not affected by alpha-amylase and proteolytic enzymes. Compared to germ agglutinin, flour agglutinin exhibits a peculiar range of cell specificity. It agglutinates several normal cell types, but has no effects on some neoplastic cells tested. Tryptic digestion of erythrocytes does not affect their susceptibility to flour agglutinin-induced agglutination.
D000372:Agglutination Tests; D001089:Arabinose / Q000032:analysis; D002460:Cell Line; D004912:Erythrocytes / Q000187:drug effects; D006386:Hemagglutination Tests; D006801:Humans; D037102:Lectins / Q000302:isolation & purification / Q000494:pharmacology; D008970:Molecular Weight; D009928:Organ Specificity; D037121:Plant Lectins; D011134:Polysaccharides; D014908:Triticum; D014364:Tryptophan / Q000494:pharmacology*; D014994:Xylose / Q000032:analysis
D037102:Lectins; D037121:Plant Lectins; D011134:Polysaccharides; D014364:Tryptophan; D014994:Xylose; D001089:Arabinose