title: N-terminal methionine in recombinant proteins expressed in two different Escherichia coli strains.
abstract: Two genes coding for chloramphenicol acetyltransferase and human interferon gamma, respectively, were overexpressed constitutively in two different strains of Escherichia coli (E. coli LE392 and E. coli XL1). The N-terminal amino acid analysis of the purified proteins showed that: (a) the N-terminal methionine is processed more efficiently in E. coli LE392 rather than in E. coli XL1 cells; (b) the N-terminal methionine is removed better from the heterologous human interferon gamma in comparison with the homologous chloramphenicol acetyltransferase protein: and (c) there is no strong correlation between the efficiency of N-terminal procession and the yield of recombinant protein.
authors: Institute of Molecular Biology, Bulgarian Academy of Science, Sofia, Bulgaria. anel@obzor.bio21.bas.bg
authors: A
authors: A
authors: Vassileva-Atanassova
authors: R
authors: R
authors: Mironova
authors: G
authors: G
authors: Nacheva
authors: I
authors: I
authors: Ivanov
mesh_terms: D000595:Amino Acid Sequence; D015500:Chloramphenicol O-Acetyltransferase / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007371:Interferon-gamma / Q000235:genetics / Q000378:metabolism*; D008715:Methionine / Q000032:analysis / Q000378:metabolism*; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D007371:Interferon-gamma; D008715:Methionine; D015500:Chloramphenicol O-Acetyltransferase