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  • Title: Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.
    Author: Hermodson M, Schmer G, Kurachi K.
    Journal: J Biol Chem; 1977 Sep 25; 252(18):6276-9. PubMed ID: 893407.
    Abstract:
    Human platelet factor 4 was purified by a method employing affinity chromatography on heparin/agarose. The amino acid sequence of the protein was determined by automatic Edman degradations and carboxypeptidase Y digestion. There are 70 amino acids in the protein with 5 of the 8 negatively charged residues clustered near the NH2 terminus and 10 of the 13 positively charged residues in clusters of 3 and 4 elsewhere in the protein. Small crystals have been obtained from ammonium sulfate solutions which give a promising preliminary x-ray diffraction pattern.
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