Abstract
The characterization and purification of the agglutinin in the Aplysia eggs capable of agglutinating vertebrate erythrocytes and marine bacteria were investigated. The agglutinin prepared from A. kurodai was specific to B cells as to human erythrocytes, while that of A. juliana was non-specific. They were independent upon divalent cations for hemagglutinating activity, though slight enhanced activity was observed by addition of Ca2+. The activity remained unchanged after the digestion with proteolytic enzymes, but was reduced partially by the treatment with 2-mercaptoethanol or periodate. The hemagglutination was inhibited by D-galacturonic acid, but not by D-glucuronic acid. The agglutinin was purified from A. kurodai eggs by affinity chromatography followed by gel-filtration. The purified preparation reacted with B cells and rabbit blood cells as low as 0.06μg/ml. The molecular weight of egg agglutinin was estimated to be 70, 000 daltons. The ratio of subunit (13, 000) to a native agglutinin was very close to 6.
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