A new mass-spectrometric C-terminal sequencing technique finds a similarity between gamma-interferon and alpha 2-interferon and identifies a proteolytically clipped gamma-interferon that retains full antiviral activity

A novel mass-spectrometric technique is described that permits the identification of the C-terminal peptide of a protein. The technique involves the incorporation of 18O into all alpha-carboxy groups liberated during enzyme-catalysed partial hydrolysis of the protein, followed by mass spectrometry t...

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Bibliographic Details
Published in:Biochemical journal 1983-11, Vol.215 (2), p.273-277
Main Authors: Rose, K, Simona, M G, Offord, R E, Prior, C P, Otto, B, Thatcher, D R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Gas Chromatography-Mass Spectrometry
Interferon Type I
Interferon-gamma
Oxygen Isotopes
Peptide Fragments - analysis
Trypsin
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Summary:A novel mass-spectrometric technique is described that permits the identification of the C-terminal peptide of a protein. The technique involves the incorporation of 18O into all alpha-carboxy groups liberated during enzyme-catalysed partial hydrolysis of the protein, followed by mass spectrometry to identify as the C-terminal peptide the only peptide that did not incorporate any 18O. The technique has been used to identify the true C-terminal tryptic peptide of a bacterially produced gamma-interferon and to distinguish it from a peptide produced by anomalous tryptic cleavage. It was found that a closely similar sequence segment of bacterially produced alpha 2-interferon undergoes an analogous cleavage. The technique was also used to identify the C-terminus of a clipped gamma-interferon that retains full antiviral activity.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2150273