Peptide mapping on HIV polypeptides expressed in Escherichia coli. Quality control of different batches and identification of tryptic fragments containing residues of aromatic amino acids or cysteine

Journal of Chromatography
S RenlundU Hellman

Abstract

Peptide mapping was used for the quality control of different batches of the recombinant HIV proteins p24 core and p24-gp41, expressed in Escherichia coli. These proteins comprise gag and env region polypeptides of the virus and may serve as suitable components in the diagnosis of HIV infections. The proteins were digested with trypsin and the mixtures were subjected to peptide mapping to prove batch equivalence of p24-gp41 and to isolate fragments of the p24-gp41 digest that differ from those of the p24 core digest. The proteins were reduced with dithiothreitol and the cysteine residues were derivatized by addition of 4-vinylpyridine. Peptide mapping was performed by means of reversed-phase high-performance liquid chromatography. Batch equivalence was proved by comparison of the maps. Peaks present in one map but not in the other were considered to be due to sequence differences or variability in digestion.

References

Jan 24, 1985·Nature·L RatnerK Baumeister
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Nov 1, 1969·Analytical Biochemistry·J F Cavins, M Friedman

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Citations

Mar 21, 1998·Journal of Pharmaceutical and Biomedical Analysis·K KannanC Karunatilake
Apr 30, 2002·Free Radical Biology & Medicine·I Dalle-DonneA Milzani
Nov 6, 2004·Nature Biotechnology·Arthur J Chirino, Anthony Mire-Sluis
Jan 15, 1999·Analytical Biochemistry·N Lundell, T Schreitmüller
Dec 9, 1997·Archives of Biochemistry and Biophysics·M A DiczfalusyS E Alexson

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