Terminal deoxynucleotidyl transferase is present in athymic nude mice

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Terminal deoxynucleotidyl transferase is found in prothymocytes

Terminal deoxynucleotidyl transferase is an enzyme which has the unique property of polymerizing polydeoxynucleotides onto a primer in the absence of a template (1,2). This enzyme is found both in the thymus and the bone marrow of birds, rodents, and humans (3-7). Whether the marrow cells that contain terminal transferase are related to thymocytes, or are on a separate pathway of differentiatio...

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Murine Terminal Deoxynucleotidyl Transferase

Terminal deoxynucleotidyl transferase (TdT) 1 is an enzyme which has the unique property of polymerizing deoxyribonucleotides onto a primer in the absence of a template (1-4) . Chang (4) first reported that TdT is present only in the thymus among various avian and mammalian tissues examined . Her finding was extended to humans by McCaffrey et al . (5), who found that the enzyme was restricted t...

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Detection of terminal deoxynucleotidyl transferase.

The recently published study of peripheral blood lymphocyte subpopulations in patients with acute immunodeficiency syndrome, by Murray et al,’ may have contributed additional insight into normal T cell ontogenesis. However, the data on terminal transferase (TdT) must be interpreted with caution. It is stated that TdT levels are especially elevated in acute lymphocytic leukemia (ALL) of T cell o...

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Induction in vivo and in vitro of terminal deoxynucleotidyl transferase by thymosin in bone marrow cells from athymic mice

Terminal deoxynucleotidyl transferase (TdT) expression in bovine serum albumin (BSA) gradient-fractionated bone marrow cells was examined in NIH Swiss nu/nu and thymectomized C57BL/6 mice. In nude mice, TdT levels were approximately 10% of those of thymus-bearing littermates. In C57BL/6 mice, thymectomy caused a time-dependent loss of TdT activity in bone marrow cells. To determine whether or n...

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Association of terminal deoxynucleotidyl transferase with Ku.

Terminal deoxynucleotidyl transferase (TdT) catalyzes the addition of nucleotides at the junctions of rearranging Ig and T cell receptor gene segments, thereby generating antigen receptor diversity. Ku is a heterodimeric protein composed of 70- and 86-kDa subunits that binds DNA ends and is required for V(D)J recombination and DNA double-strand break (DSB) repair. We provide evidence for a dire...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 1977

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/4.2.457