Four different vitellogenin proteins of Xenopus identified by translation in vitro.
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.
D000818:Animals; D003488:Cyanogen Bromide; D004967:Estrogens / Q000494:pharmacology; D007700:Kinetics; D008074:Lipoproteins / Q000096:biosynthesis*; D008099:Liver / Q000378:metabolism*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D014176:Protein Biosynthesis / Q000187:drug effects; D012333:RNA, Messenger / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism; D014819:Vitellogenins / Q000096:biosynthesis*; D014981:Xenopus
D004967:Estrogens; D008074:Lipoproteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D012333:RNA, Messenger; D014819:Vitellogenins; D003488:Cyanogen Bromide