Open AccessFour Different Vitellogenin Proteins of Xenopus Identified by Translation in vitro
Author(s) -
JAGGI Rolf B.,
FELBER Barbara K.,
MAURHOFER Susanne,
WEBER Rudolf,
RYFFEL Gerhart U.,
Muellener Daniel
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04800.x
Subject(s) - vitellogenin , cyanogen bromide , phosvitin , reticulocyte , vitellogenins , translation (biology) , xenopus , serine , messenger rna , protein biosynthesis , cleavage (geology) , chemistry , in vitro , biochemistry , microbiology and biotechnology , biology , peptide sequence , enzyme , oocyte , gene , embryo , paleontology , protein kinase a , vitellogenesis , fracture (geology)
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.