Amino acid sequence of human platelet factor 4.

作者：Thomas F. Deuel, P S Keim, Martha C. Farmer, Robert L. Heinrikson · 发表于：Proceedings of the National Academy of Sciences · 年份：1977 · DOI：10.1073/pnas.74.6.2256 · 被引用次数：316 · 研究领域：Proteoglycans and glycosaminoglycans research、Blood properties and coagulation、Platelet Disorders and Treatments

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.