Interactions of plasminogen and fibrinogen with model silica glass surfaces: Adsorption from plasma and enzymatic activity studies
✍ Scribed by Woodhouse, K. A. ;Weitz, J. I. ;Brash, J. L.
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 920 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0021-9304
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✦ Synopsis
The adsorption of fibrinogen and plasminogen from plasma to silica glass, sulfonated silica glass, and lysinederivatized silica glass has been investigated. The data indicate that the sulfonated material has a high affinity for both fibrinogen and plasminogen, but that the ratio of plasminogen to fibrinogen is greater on the lysinederivatized surface. The adsorption data also suggest plasminogen as a possible contributor to the fibrinogen Vroman effect, whereby initially adsorbed fibrinogen is displaced from the surface. The plasmin activity of plasminogen adsorbed to the lysine-derivatized silica glass and its sulfonated precursor was assessed by both a chromogenic substrate assay and a radioimmunoassay for the plasmin cleavage product of fibrinogen, the BP 1-42 peptide. The data indicate that 1) the adsorbed plasminogen is not inherently plasmin-like; 2) the enzymatic activity associated with the bound plasminogen is significantly enhanced on both surfaces in the presence of