ABSTRACT
Mouse epidermal growth factor (EGF) is under investigation as a deflecting agent for sheep. Substantial quantities of the pure protein are required for these studies and to supply this need a gene for the protein was synthesized and inserted into plasmid vectors to direct the expression of EGF polypeptide, or fusion proteins containing the EGF peptide sequence, in transformed Escherichia coli. Mature EGF was released by lysine specific proteolysis of a fusion protein consisting of part of the E. coli TrpE protein, a lysine linker and EGF polypeptide. The EGF was purified and characterized and was found to be biologically active.
Subject(s)
Epidermal Growth Factor/biosynthesis , Escherichia coli/genetics , Genes, Bacterial , Genes, Synthetic , Base Sequence , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Epidermal Growth Factor/genetics , Epidermal Growth Factor/isolation & purification , Lysine/metabolism , Oligodeoxyribonucleotides/biosynthesis , PlasmidsABSTRACT
Cloned cDNA molecules from three serotypes of FMDV have been sequenced around the VP1-coding region. The predicted amino acid sequences for VP1 were compared with the published sequences and variable regions identified. The amino acid sequences were also analysed for hydrophilic regions. Two of the variable regions, numbered 129-160 and 193-204 overlapped hydrophilic regions, and were therefore identified as potentially immunogenic. These regions overlap regions shown by others to be immunogenic.
Subject(s)
Antigens, Viral/genetics , Aphthovirus/immunology , Cloning, Molecular , DNA/metabolism , Genes, Viral , Amino Acid Sequence , Aphthovirus/genetics , Base Sequence , SerotypingABSTRACT
cDNAs coding for the amino and carboxy termini of two trypanosome variant surface glycoproteins (VSGs) have been sequenced. The results indicate that VSGs are synthesised with hydrophobic amino-terminal leader and carboxy-terminal tail sequences which are absent from purified mature VSGs.
