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Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions
Open accessAbstract
Fibronectin was purified from human plasma by affinity chromatography under nondenaturing conditions. The method was based on the previously known binding of fibronectin to gelatin. The novel features of our method are the use of arginine in the elution of fibronectin from immobilized gelatin [Vuento & Vaheri (1978) Biochem. J. 175, 333-336] and the use of arginine-agarose as second affinity step. The purified protein was homogeneous as judged by polyacrylamide-gel electrophoresis, analytical ultracentrifugation and two-dimensional immunoelectrophoresis. The yield was 60%. We propose that the method would be useful in preparation of fibronectin for studies on its biological activities, where it is important that the protein is obtained in a native state.
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Cited by
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Panayotou, G., End, P., Aumailley, M., Timpl, R., & Engel, J. (1989) · Cell · doi:10.1016/0092-8674(89)90987-2 · Cited by 341
Wann, E. R., Gurusiddappa, S., & Höök, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13863 · Cited by 300
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Xing, H., Lee, H., Luo, L., & Kyriakides, T. R. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107421 · Cited by 302
The O75X adhesin of uropathogenic Escherichia coli is a type IV collagen‐binding protein
Westerlund, B., Kuusela, P., Risteli, J., Risteli, L., Vartio, T., Rauvala, H., Virkola, R., & Korhonen, T. K. (1989) · Molecular Microbiology · doi:10.1111/j.1365-2958.1989.tb00178.x · Cited by 142
Metadata
- Authors
- Vuento, M., & Vaheri, A.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1979-11-01
- Volume
- 183
- Issue
- 2
- Pages
- 331-337
- ISSN
- 0264-6021 (ISSN-L)
- OpenAlex
- W1820433806
- Cited by
- 545
- References
- 0
- FWCI
- 14.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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