Unknown

Dataset Information

0

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.


ABSTRACT: 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.

SUBMITTER: Rose K 

PROVIDER: S-EPMC1152394 | biostudies-other | 1983 Nov

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC2195910 | biostudies-literature
| S-EPMC6120754 | biostudies-literature
| S-EPMC2258722 | biostudies-literature
| S-EPMC3868162 | biostudies-literature
| S-EPMC7112673 | biostudies-literature
| S-EPMC3416106 | biostudies-literature
| S-EPMC3348177 | biostudies-literature
| S-EPMC5333814 | biostudies-literature
| S-EPMC3165780 | biostudies-literature
| S-EPMC4279735 | biostudies-literature