XB-ART-31354
Eur J Biochem
1980 Aug 01;1092:343-7.
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Four different vitellogenin proteins of Xenopus identified by translation in vitro.
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Kinetic analysis of vitellogenin mRNA translation in a cell-free reticulocyte lysate translation system revealed that a serine-rich sequence, most probably containing the phosvitin molecule, is located toward the end of the translational product and therefore resides near to the carboxy terminus of the vitellogenin molecule. Translation of the four different vitellogenin mRNAs in vitro and cleavage of the translational products with cyanogen bromide revealed that vitellogenin consists of four different polypeptides, each containing a serine-rich sequence toward its carboxy terminus.
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Species referenced: Xenopus
Genes referenced: vtga2