Lamprey produced agglutinins in high titer against Brucella organisms and the H antigens of human “O” cells. The antibody was shown to be labile at room temperature. The lamprey immunoglobulin was purified using Bio-Gel A 1.5 column and DE 52-cellulose column fractionation. Both purified immunoglobulin and antibody activity of serum were shown to have the electrophoretic mobility of an alpha globulin, a sedimentation velocity of 9S and a molecular weight of approximately 300,000. These characteristics indicate that the lamprey immunoglobulin is unique.
No takes yet. Share an insight, caveat, or question.
Pollara et al. (1970) studied this question.