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Platelet-derived growth factor: purification and partial characterization.

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Heldin, C H, Westermark, B, Wasteson, A·1979·Proceedings of the National Academy of Sciences

Abstract

A cationic protein that stimulates DNA synthesis in human cultured cells was isolated from human platelets by ion exchange chromatography, hydrophobic chromatography, gel chromatography, and gel electrophoresis in sodium dodecyl sulfate. The electrophoretic behavior of biologically active or radioiodinated and reduced growth factor indicated that the native protein (approximately 30,000 daltons) was composed of two different polypeptides (approximately 13,000-14,000 and 16,000-17,000 daltons, respectively) linked via reduction-susceptible bonds. The stimulatory activity on human glial cells of the purified product at a concentration of approximately 4 ng/ml (0.13 nM) was equal to that of 1% human serum.

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Metadata

Authors
Heldin, C. H., Westermark, B., & Wasteson, A.
Venue
Proceedings of the National Academy of Sciences
Published
1979-08
Volume
76
Issue
8
Pages
3722-3726
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2081203911
Cited by
429
References
0
FWCI
10.04
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Platelet-derived growth factor: purification and partial characterization. https://app.cochat.ai/papers/10.1073/pnas.76.8.3722
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Heldin, C. H., Westermark, B., & Wasteson, A. (1979). Platelet-derived growth factor: purification and partial characterization. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.76.8.3722

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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.