Adsorption of proteins to surfaces in seawater
1989; Elsevier BV; Volume: 27; Issue: 3-4 Linguagem: Inglês
10.1016/0304-4203(89)90048-0
ISSN1872-7581
AutoresDavid L. Kirchman, Diane Henry, S. C. Dexter,
Tópico(s)Advanced Biosensing Techniques and Applications
ResumoAdsorption of two proteins, bovine serum albumin and ribulose-1,5-bisphosphate carboxylase, (RuBPcase), onto a variety of surfaces was examined. Protein adsorption was rapid, but was irreversible in seawater only when bulk protein concentrations were low (<10 μg ml−1). Adsorption was consistently higher onto Parafilm (a surface with a low work of adhesion and high hydrophobicity) than onto glass (high work of adhesion and low hydrophobicity). When a variety of surfaces were tested, there was a significant negative relationship between RuBPcase adsorption and work of adhesion. For all surfaces, adsorption was higher in seawater than in low ionic strength buffer. The high adsorption in seawater was a result of the high salt concentration of seawater. Low concentrations of both NaCl and MgCl2 increased adsorption, but MgCl2, was more effective. The relationship between work of adhesion and adsorption indicates that hydrophobic interactions are important in determining protein adsorption, especially at high salinities.
Referência(s)