title: Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.
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.
mesh_terms: D000595:Amino Acid Sequence; D001779:Blood Coagulation Factors / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D003460:Crystallization; D006801:Humans; D010446:Peptide Fragments; D010978:Platelet Factor 4 / Q000302:isolation & purification*
chemical_list: D001779:Blood Coagulation Factors; D010446:Peptide Fragments; D010978:Platelet Factor 4