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. 1977 Jun;74(6):2256–2258. doi: 10.1073/pnas.74.6.2256

Amino acid sequence of human platelet factor 4.

T F Deuel, P S Keim, M Farmer, R L Heinrikson
PMCID: PMC432148  PMID: 267922

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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