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Cited by 310

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Amino acid sequence of human platelet factor 4.

Open access
Deuel, T F, Keim, P S, Farmer, M, Heinrikson, R L·1977·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Deuel, T. F., Keim, P. S., Farmer, M., & Heinrikson, R. L.
Venue
Proceedings of the National Academy of Sciences
Published
1977-06
Volume
74
Issue
6
Pages
2256-2258
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2030344520
Cited by
310
References
0
FWCI
15.67
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Amino acid sequence of human platelet factor 4. https://app.cochat.ai/papers/10.1073/pnas.74.6.2256
The paper
Deuel, T. F., Keim, P. S., Farmer, M., & Heinrikson, R. L. (1977). Amino acid sequence of human platelet factor 4. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.6.2256

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.