AMINO-ACID SEQUENCE OF HUMAN PLATELET FACTOR 4
AMINO-ACID SEQUENCE OF HUMAN PLATELET FACTOR 4
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DOI：
10.1073/pnas.74.6.2256
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发表时间：
1977-01-01
影响因子：
11.1
通讯作者：
HEINRIKSON, RL
中科院分区：
文献类型：
--
作者：
DEUEL, TF;KEIM, PS;HEINRIKSON, RL
人血小板因子4，一种结合肝素的蛋白质，被纯化至表观均一性，并测定了该蛋白质的完整氨基酸序列。70个残基的多肽链不含甲硫氨酸、色氨酸或苯丙氨酸，仅含单个酪氨酰残基。序列分析表明，一个高度负电荷的氨基末端区域。多肽的羧基末端区域是不寻常的，因为它包含带正电荷和疏水性氨基酸对的重复聚类;初步证据表明，该结构域可能在肝素的结合中发挥作用。
Human platelet factor 4, a protein that binds heparin, was purified to apparent homogeneity and the complete amino acid sequence of the protein was 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.