Four Different Vitellogenin Proteins of Xenopus Identified by Translation in vitro

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Abstract
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 the carboxy terminus of the vitellogenin molecule. Translation of the 4 different vitellogenin mRNA in vitro and cleavage of the translational products with cyanogen bromide revealed that vitellogenin consists of 4 different polypeptides, each containing a serine-rich sequence toward its carboxy terminus.