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Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.

1977; Elsevier BV; Volume: 252; Issue: 18 Linguagem: Inglês

10.1016/s0021-9258(17)39951-9

1083-351X

Mark A. Hermodson, Gottfried Schmer, Kotoku Kurachi,

Platelet Disorders and Treatments

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.