Isolation and Characterization of a New Agglutinin in the Red Alga Palmaria palmata (L.) O. Kuntze

Publisher Website
Google Scholar
Abstract
Extracts of the red alga P. palmata contained an agglutinin which reacted with rabbit and horse erythrocytes and with proteolytic enzyme-treated human red blood cells. It selectively agglutinated mouse leukemia cells L5178Y, but not L1210. The hemagglutinating activity was stable between pH 6-10 and was independent of divalent cations. The activity was inhibited by a high concentration of N-acetylneuraminic acid and D-glucuronic acid. The active component was purified and found to be a glycoprotein having a MW of 43,000 daltons, which dissociates into subunits of equal size (20,000 daltons). The isoelectric point was estimated to be 4.6. It contained high amounts of serine, glycine and aspartic acid, but no half cystine.