title: Amino acid sequence of human platelet factor 4.
abstract: Human platelet factor 4, a protein that binds heparin, has been purified to apparent homogeneity and the complete amino acid sequence of the protein has been determined. The 70-residue polypeptide chain contains no methionine, tryptophan, or phenylalanine, and contains only a single tyrosyl residue. The sequence analysis demonstrates a highly negatively charged amino-terminal region. The carboxyl-terminal region of the polypeptide is unusual in that it contains a repetitive clustering of positively charged and hydrophobic pairs of amino acids; preliminary evidence suggests that this domain may play a role in the binding of heparin.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001779:Blood Coagulation Factors; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010978:Platelet Factor 4
chemical_list: D000596:Amino Acids; D001779:Blood Coagulation Factors; D010446:Peptide Fragments; D010978:Platelet Factor 4
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