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Isolation, purification and biochemical characterization of E-receptors on surfaces of porcine peripheral lymphocytes.

A report on the study of isolation, purification and biochemical characterization of two glycoproteins, designated as Gp1 and Gp2, with E-receptor activity from the surfaces of porcine peripheral lymphocytes is presented. The molecular weights of Gp1 and Gp2 have been found to be 58,000 and 29,000 Daltons, and the isoelectric points 6.8 and 5.5 respectively. N-terminal amino acid residues of Gp1 are glycine and alanine, and that of Gp2 is glycine. Monospecific rabbit anti-Gp1 antiserum shown to inhibit E-rosette formation of porcine lymphocytes has been obtained. The present paper gives for the first time the evidence that the E-receptor of porcine lymphocytes, Gp1 appears to have cross antigenicity with that of human lymphocytes. Further studies of Gp2 in detail and its relationship to Gp1 will be published elsewhere.