Structure elucidation of a purple peptide found during the purification of a recombinant protein from Escherichia coli.

نویسندگان

  • A W Guzzetta
  • P Clark
  • R Tappe
  • H Budzikiewicz
چکیده

A purple substance (4) partially co-purified with a recombinant human B-type natriuretic peptide (hBNP), following an E. coli fermentation. The structure of the compound was elucidated by NMR, electrospray and FAB mass spectrometry. The chromophore is a 1,4-naphthoquinone condensed with the N-terminal cysteine of a heptapeptide by its NH2- and SH-groups to form a dihydro-thiazine ring. The peptide sequence was determined as Cys-Lys-Val-Leu-Arg-Arg-His by mass spectrometric techniques. CID and data base matching identified it as the C-terminus of the 32-amino-acid recombinant peptide hBNP. This modification of an N-terminal Cys may be a more general phenomenon with implications for the production of heterologous proteins by microorganisms.

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عنوان ژورنال:
  • Zeitschrift fur Naturforschung. C, Journal of biosciences

دوره 54 3-4  شماره 

صفحات  -

تاریخ انتشار 1999