Abstract
In this study, we report a strong interaction between two contiguous proteolytic fragments of fibronectin, each having a mass of about 16 kDa. This interaction was stable in 4 M NaCl and 4 M urea and dissociation of the two fragments required buffers containing 0.5% sodium dodecyl sulphate. After purification, these peptides maintained their ability to interact when mixed. One fragment was made up of type III repeat 4 and part of 5, the other by repeat 6 and part of 5. Such strong interaction between two fibronectin regions may play a role in fibronectin conformation as well as during fibronectin fibril formation.
| Original language | English |
|---|---|
| Pages (from-to) | 745-748 |
| Number of pages | 4 |
| Journal | Biochemistry and Cell Biology |
| Volume | 74 |
| Issue number | 6 |
| Publication status | Published - 1996 |
Keywords
- Fibronectin
- Type iii repeats interaction
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Cell Biology
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Cite this
Carnemolla, B. (1996). Novel self-association fibronectin sites. Biochemistry and Cell Biology, 74(6), 745-748.