Isolation and partial characterization of a 48-kDa protein which is induced in normal lymphocytes upon mitogenic stimulation.
A 48-kDa protein (p48) crossreactive with an antiserum directed against the 12 C-terminal amino acids of the human cellular myc gene-encoded protein was isolated from a Burkitt lymphoma cell line. The p48 protein is a basic protein and has a cytoplasmic localization. An antiserum prepared against purified p48 reacts specifically with a 48-kDa protein present in a variety of mouse and human cells. This polypeptide is detected at very low levels in normal, resting, peripheral blood lymphocytes, but is induced several-fold by stimulation with either concanavalin A or pokeweed mitogen. The association of p48 induction with a proliferative response and the crossreactivity with the cellular myc protein are discussed.
D000818:Animals; D002051:Burkitt Lymphoma; D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D007120:Immunochemistry; D007525:Isoelectric Focusing; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000378:metabolism*; D051379:Mice; D008934:Mitogens / Q000494:pharmacology*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification*; D013347:Subcellular Fractions / Q000378:metabolism
D008934:Mitogens; D009363:Neoplasm Proteins; D011506:Proteins