Labile disulfide bonds are common at the leucocyte cell surface.

ABSTRACT: Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not exposed at the protein surface. We have developed a proteomic/mass spectrometry method to screen for and identify non-structural, redox-labile disulfide bonds in leucocyte cell-surface proteins. These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin. The proteins identified include integrins, receptors, transporters and cell-cel

SUBMITTER: Metcalfe C 

PROVIDER: S-EPMC3352085 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature