The lethal protein from Kintoki beans (Phaseolus vulgaris) identified as a lectin.

Abstract

A glycoprotein isolated from Kintoki beans (Phaseolus vulgaris cultivar Kintoki) agglutinated human erythrocytes of all types and erythrocytes of rat, rabbit, sheep, and mouse. The lectin activity was not affected by 1 hr heating at 60 degrees C, but decreased slightly on heating for the same period at 70-80 degrees C and markedly at 90-100 degrees C. The activity was inhibited by galactose, lactose, N-acetyl galactosamine and fetuin. The inhibition was, however, weak, as often found for nonspecific lectins. The activity did not change when tyrosine residues or small parts of amino groups were modified, but decreased considerably when histidine residues or carboxyl groups were modified. This lectin was found to be relatively resistant to trypsin, and, particularly, to pepsin. All mice died within 48 hr when 200 microgram lectin per gram body weight was injected intraperitoneally and 14 microgram intravenously. The toxic activity changed in parallel with the lectin activity upon various treatments of the glycoprotein. In addition, blood analyses of injected mice suggested that the toxicity might be developed by the action of the lectin on blood cells.