The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable
Open accessAbstract
At least 50% of the actin in resting human platelets is unpolymerized, and the bulk of this unpolymerized actin is complexed with a recently identified acidic, heat-stable 5-kDa peptide, named "Fx." Purified Fx binds stoichiometrically to muscle G-actin, forming a complex identifiable by nondenaturing polyacrylamide gel electrophoresis. Formation of the complex inhibits salt-induced polymerization of G-actin. Here we report that Fx is indistinguishable from thymosin beta 4, an acidic, heat-stable 5-kDa peptide first isolated from calf thymus and thought to be a thymic hormone. The complete amino acid sequence of Fx was determined and was found to be identical with that of thymosin beta 4. Authentic thymosin beta 4 is functionally equivalent to Fx, forming a 1:1 complex with actin monomers and inhibiting polymerization. The widespread distribution and high intracellular concentration of thymosin beta 4 (Fx) strongly suggest that it plays a significant role in regulating actin polymerization in many cell types.
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Cites
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
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Bock-Marquette, I., Saxena, A., White, M. D., Michael DiMaio, J., & Srivastava, D. (2004) · Nature · doi:10.1038/nature03000 · Cited by 657
The Extracellular Actin-Scavenger System and Actin Toxicity
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GOLDSTEIN, A., HANNAPPEL, E., & KLEINMAN, H. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.07.004 · Cited by 250
Metadata
- Authors
- Safer, D., Elzinga, M., & Nachmias, V. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-03
- Volume
- 266
- Issue
- 7
- Pages
- 4029-4032
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1795265328
- Cited by
- 353
- References
- 1
- FWCI
- 11.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable. https://app.cochat.ai/papers/10.1016/s0021-9258(20)64278-8
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- Safer, D., Elzinga, M., & Nachmias, V. T. (1991). Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)64278-8
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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.
