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Title: Cell-free translation of the messenger RNA for calf terminal deoxynucleotidyltransferase. Author: Wolf SC, Kourides IA, Good RA, Silverstone AE. Journal: J Biol Chem; 1982 Apr 25; 257(8):4013-5. PubMed ID: 6175635. Abstract: Poly(A)-rich RNA has been isolated from calf thymus and translated in vitro in a rabbit reticulocyte translation system. Three peptides with Mr = 58,000, 33,000, and 13,000 were specifically immunoprecipitated from the translation products with calf terminal deoxynucleotidyltransferase antiserum. An oligo(dT)-purified preparation of calf terminal transferase competed with only the Mr = 58,000 peptide in the immunoprecipitation reaction. The anti-terminal transferase serum did not precipitate a Mr = 58,000 peptide from translation products of spleen or liver mRNA, but it did precipitate the Mr = 33,000 and 13,000 peptides from products of spleen mRNA and a Mr = 13,000 peptide from products of liver mRNA. In addition, when an affinity-purified antibody to calf terminal transferase was used, only a Mr = 58,000 peptide was immunoprecipitated from the translation products of calf thymus mRNA, and none was immunoprecipitated from spleen or liver mRNA products. This antibody also precipitated a Mr = 58,000 peptide from the cell lysates of calf thymocytes labeled in vitro with [35S]methionine. These results demonstrate that calf terminal transferase is biosynthesized as a Mr = 58,000 peptide.[Abstract] [Full Text] [Related] [New Search]