Thymus leukemia (TL) alloantigenic activity was solubilized by papain proteolytic digestion from intact RADA1 tumor cells. If the cells were labeled with amino acids and fucose, the TL alloantigen could be isolated as a doubly labeled glycoprotein fragment by indirect precipitation from the papain digest. This TL glycoprotein fragment was approximately the same mol wt as the papain-digested H-2.4 alloantigen fragment as judged by chromatography on Sephadex G-150 in sodium dodecyl sulfate. The carbohydrate chain of the TL glycoprotein obtained by exhaustive pronase digestion behaved as a glycopeptide of approximately 4,500 mol wt, as compared with the glycopeptide of the H-2.4 alloantigen that had a mol wt of about 3,500. Thus, the TL alloantigen can be solubilized by papain digestion as a glycoprotein fragment similar in mol wt to the H-2 alloantigen glycoprotein fragment. The carbohydrate chain of the TL glycoprotein is larger than the H-2 carbohydrate chain.
SOME BIOCHEMICAL PROPERTIES OF THYMUS LEUKEMIA ANTIGENS SOLUBILIZED FROM CELL MEMBRANES BY PAPAIN DIGESTION
Takashi Muramatsu, Stanley G. Nathenson, Edward A. Boyse, Lloyd J. Old; SOME BIOCHEMICAL PROPERTIES OF THYMUS LEUKEMIA ANTIGENS SOLUBILIZED FROM CELL MEMBRANES BY PAPAIN DIGESTION . J Exp Med 1 May 1973; 137 (5): 1256–1262. doi: https://doi.org/10.1084/jem.137.5.1256
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