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. 1986 Feb 13;134(3):1238-44.
doi: 10.1016/0006-291x(86)90383-9.

Isolation and partial characterization of a 48-kDa protein which is induced in normal lymphocytes upon mitogenic stimulation

A Giallongo, S Feo, L C Showe, C M Croce

Isolation and partial characterization of a 48-kDa protein which is induced in normal lymphocytes upon mitogenic stimulation

A Giallongo et al. Biochem Biophys Res Commun. .

Abstract

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.

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