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TJ Kunicki, PJ Newman, DL Amrani and MW Mosesson
Conditions were developed in which 80% to 90% of platelet fibrinogen could
be routinely purified in nondegraded form from the fluid phase of platelet
suspensions stimulated with the calcium ionophore, A23187, in the presence
of calcium, leupeptin, and prostaglandin E1. Fibrinogen was separated from
other released proteins by chromatography on diethylaminoethanol
(DEAE)-cellulose using a continuous pH and ionic strength gradient.
Purified platelet fibrinogen, greater than 98% homogeneous by
immunoelectrophoresis and sodium-dodecyl sulfate- polyacrylamide gel
electrophoresis (SDS-PAGE), consisted of intact A alpha, B beta and gamma A
chains, but not gamma' chains, and was 95% to 96% clottable. Platelet
fibrinogen was shown to compete for the binding of radiolabeled plasma
fibrinogen to ADP-activated platelets in a manner identical to that of
unlabeled plasma fibrinogen itself. Also, at equivalent protein
concentrations, platelet and plasma fibrinogens supported platelet
aggregation to an equivalent extent. Based upon these results, we conclude
that there is no significant difference between platelet and plasma
fibrinogen with respect to their size, their clottability, their affinity
for the activated platelet fibrinogen receptor, or their capacity to
support subsequent platelet aggregation.
This article has been cited by other articles:
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| Copyright © 1985 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
