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Human platelet basic protein. Its relation to low affinity platelet factor 4 and beta-thromboglobulin.

K G Varma·S Niewiarowski·J C Holt·B Rucinski·D Paul
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Abstract

Human beta-thromboglobulin, low affinity platelet factor 4 and platelet basic protein have been purified to homogeneity from the material released by thrombin-stimulated platelets. Purification steps included isoelectric focusing and heparin-agarose chromatography. Antibodies against each of these proteins have been raised in rabbits. Antigenic identity of the proteins has been demonstrated in radioimmunoassay using 125I-labelled platelet basic protein or 125I-labelled low affinity platelet factor 4 and a variety of antibodies. The molecular weight of platelet basic protein estimated by gel filtration in 6 M guanidine hydrochloride using Sepharose 6B corresponded to approx. 10 000 daltons, slightly higher than that of beta-thromboglobulin (8851 daltons) and low affinity platelet factor 4 (9278 daltons). These findings raise the possibility that the formation of low affinity platelet factor 4 beta-thromboglobulin may be a consequence of the action of proteolytic enzymes on platelet basic protein.

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Amino Acid SequenceAnimalsAntibody SpecificityBeta-GlobulinsBlood Coagulation FactorsBlood PlateletsBlood ProteinsChromatography, GelEpitopesGuanidinesHumansMolecular WeightPeptidesRabbitsRadioimmunoassaybeta-ThromboglobulinJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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K G Varma, S Niewiarowski, J C Holt, B Rucinski, D Paul. 1982-02-04. Human platelet basic protein. Its relation to low affinity platelet factor 4 and beta-thromboglobulin.. https://doi.org/10.1016/0167-4838(82)90304-1

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