Abstract
Platelet plasma membrane glycoproteins. Evidence for the presence of nonequivalent disulfide bonds using nonreduced-reduced two-dimensional gel electrophoresis.
Highlights
Proteins on the surface of human platelets were labeled by the lactoperoxidase-iodination procedure
The polypeptides were separated by a two-dimensional sodium dodecyl sulfate electrophoretic technique in which the solubilized platelet polypeptides were electrophoresed first with disulfide bonds intact followed by electrophoresis in the second dimension after disulfide reduction
We report an improved method for separation of the platelet membrane glycoproteins
Summary
Proteins on the surface of human platelets were labeled by the lactoperoxidase-iodination procedure. The polypeptides were separated by a two-dimensional sodium dodecyl sulfate electrophoretic technique in which the solubilized platelet polypeptides were electrophoresed first with disulfide bonds intact followed by electrophoresis in the second dimension after disulfide reduction. Analysis of the twodimensional separation of iodinated platelet proteins revealed that seven polypeptides with molecular weights from. Ia, IIa, III, and the larger subunit of IIb, gave evidence for intramolecular disulfide bonds as well. Nonequivalence of these various bonds in the sodium dodecyl sulfate-denatured state was evident, since intermediate states of reduction were readily obtained. Adhering platelets undergo a release reaction, whereby the contents of their storage organelles are extruded outside the cell
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