Susceptibility of platelet alpha-actinin to a Ca2+-activated neutral protease |
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Authors: | Y Gache F Landon H Touitou A Olomucki |
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Affiliation: | Laboratoire de Biochimie Cellulaire, Collège de France, 11, Place Marcelin Berthelot, 75231 Paris Cedex 05, France |
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Abstract: | Purified alpha-actinin from human platelets was digested with Ca2+-activated protease from muscle. The alpha subunit (Mr = 100 kDa) was degraded into a unique polypeptide b of slightly lower molecular mass. In fresh platelets, only the a subunit was detected by immunoblotting techniques, while in out-dated platelets, both a and b polypeptides were present. Since a similar conversion of a to b occurs in vitro as in whole platelets, it can be assumed that, in platelets, alpha-actinin is cleaved by the endogenous Ca2+-activated protease. |
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Keywords: | ME 2-mercaptoethanol PAGE polyacrylamide gel electrophoresis SDS sodium dodecyl sulfate ABP actin binding protein |
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