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Published January 25, 1980 | Published
Journal Article Open

Biosynthesis of Murine Terminal Deoxynucleotidyltransferase

Abstract

An immunoprecipitation assay for measuring synthesis of murine terminal deoxynucleotidyltransferase (EC 2.7.7.31) has been developed using rabbit antiserum to calf terminal transferase. The antiserum precipitates a single Mr = 60,000 polypeptide (TdT-60) from all cell lines and tissues that contain enzymologically demonstrable terminal transferase. This polypeptide is not precipitated from labeled extracts of cells that lack terminal transferase by enzymological criteria. TdT-60 fractionates with terminal transferase during phosphocellulose chromatography and sediments with it in a sucrose gradient. TdT-60 is not detectably processed to lower molecular weight polypeptides, and terminal transferase activity sediments as a Mr = 60,000 activity; thus, we believe it to be the active form of terminal transferase. Using this assay we have demonstrated that terminal transferase is synthesized in both the murine thymus and the bone marrow at a rate proportional to its biochemically measured steady state level. After cortisone treatment of mice, the Mr = 60,000 polypeptide disappears from the thymus and then reappears as the thymus begins to be repopulated.

Additional Information

© 1980 American Society for Biochemistry and Molecular Biology. Received for publication, July 2, 1979, and in revised form, September 21, 1979. T his work was supported by Grant CA-14051 from the National Cancer Institute and Contract NOl-CP-53562 from the Division of Cancer Cause and Prevention, National Cancer Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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August 19, 2023
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