Abstract
Human plasma fibronectin forms spread monolayers at the air/solution interface. The properties of these monolayers have been examined as a function of the composition, pH, and temperature of the aqueous phase by using low-pressure surface manometry and surface potentials. From the isotherms the molecular weight of HPFN was determined as 4.5 × 105 daltons, in agreement with the expected double-chain form of the protein. The surface densities at the highest pressures studied strongly indicate extensive folding. The second virial coefficients at 25 and 10 °C and the entropies of compression suggest several folding and packing patterns depending on the charge state of the glycoprotein.
Original language | English (US) |
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Pages (from-to) | 47-50 |
Number of pages | 4 |
Journal | Langmuir |
Volume | 2 |
Issue number | 1 |
DOIs | |
State | Published - 1986 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- General Materials Science
- Condensed Matter Physics
- Surfaces and Interfaces
- Spectroscopy
- Electrochemistry