SOME BIOLOGICAL PROPERTIES OF PINELLIN
摘要
Pinellin, a crystalline plant protein from Pinellia ternata, exhibits cell aggluti-nation and mitogenic activity. Pinellin agglutinates erythrocytes from such species asthe sheep, dog, cat, rabbit, guinea pig, rat, mice and pigeon but does not agglutinateerythrocytes of man, monkey, pig, chicken, duck, goose, tortoise, toad and eel. Theresults show that hemagglutination of pinellin is species specific with regard to theblood donor. In hapten inhibition of hemagglutination of the many monosaccharides, disaccha-rides, polysaccharides and glycoproteins that have been tested, only mannan andthyroglobulin which contain an oligomannoside core inhibited the hemagglutinationof rabbit erythrocytes by pinellin. The evidence suggested that pinellin binds onlyto mannose and that the size of the binding site is larger than a monosaccharide.Pinellin is the unique lectin which binds to mannose without also binding to glucose. In addition to erythrocytes, pinellin also agglutinates splenocytes, Ehrlich ascitiecells and Hep A hepatoma ascitic cells from mouse and cultured human hepatomacells. Pinellin does not agglutinate epididymal adipocytes of the rat and omentummajus of the pig, though it binds to them. These results indicate that the cellagglutination of pinellin not only exihibited species specificity but also cell typespecificity. Pinellin is a mitogen for rabbit peripheral lymphocytes and mouse spleenlymphocytes but not for human peripheral lymphocytes. Thus there is with pinellinalso species specificity in mitogenic action.