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Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils
Open accessAbstract
Fibrillin, a connective tissue macromolecule (Mr = 350,000) which is normally insoluble in its tissue form, has been purified from the medium of human skin fibroblast and ligament cells in culture. Analysis of the amino acid composition indicates that fibrillin contains approximately 14% cysteine, of which one-third appears to be in the free reactive sulfhydryl form. Electron microscopic images of fibrillin reveal an extended, flexible molecule approximately 148 nm long and 2.2 nm wide. These length measurements are consistent with shape calculations based upon velocity sedimentation data. It is likely that the material we have purified from cell culture medium represents monomeric fibrillin consisting of a single polypeptide chain. Additional ultrastructural immunohistochemical data presented here suggest a model for the parallel, head-to-tail alignment of fibrillin molecules in microfibrils.
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Isogai, Z., Ono, R. N., Ushiro, S., Keene, D. R., Chen, Y., Mazzieri, R., Charbonneau, N. L., Reinhardt, D. P., Rifkin, D. B., & Sakai, L. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209256200 · Cited by 548
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Metadata
- Authors
- Sakai, L. Y., Keene, D. R., Glanville, R. W., & Bächinger, H. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 266
- Issue
- 22
- Pages
- 14763-14770
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1503363172
- Cited by
- 288
- References
- 0
- FWCI
- 7.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Sakai, L. Y., Keene, D. R., Glanville, R. W., & Bächinger, H. P. (1991). Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)98752-1
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
