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

Biochim Biophys Acta. 1982 Feb 4;701(1):7-11. doi: 10.1016/0167-4838(82)90304-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibody Specificity
  • Beta-Globulins / immunology*
  • Blood Coagulation Factors / immunology*
  • Blood Platelets / immunology*
  • Blood Proteins / immunology*
  • Chromatography, Gel
  • Epitopes / immunology*
  • Guanidines
  • Humans
  • Molecular Weight
  • Peptides*
  • Rabbits / immunology
  • Radioimmunoassay
  • beta-Thromboglobulin / immunology*


  • Beta-Globulins
  • Blood Coagulation Factors
  • Blood Proteins
  • Epitopes
  • Guanidines
  • Peptides
  • beta-Thromboglobulin
  • connective tissue-activating peptide
  • low affinity platelet factor 4