The behavior of some model proteins at solid-liquid interfaces 2. Sequential and competitive adsorption

  • Arai T
  • Norde W
  • 50

    Readers

    Mendeley users who have this article in their library.
  • 97

    Citations

    Citations of this article.

Abstract

The proteins used in this study, lysozyme, ribonuclease, myoglobin and α-lactalbumin, have similar molecular masses (ca 15 000 dalton) and similar dimensions, but they differ with respect to isoelectric point and structure stability. Sequential and competitive adsorption experiments have been performed in a systematic way using sorbent surfaces of varying hydrophobicity and charge density. Adsorbed and desorbed amounts were calculated from changes in the protein solution concentrations as determined by FPLC. In addition, electrophoretic mobilities of bare and protein-covered sorbent particles were measured. Sequential and competitive adsorption of lysozyme, ribonuclease and myoglobin are primarily influenced by electrostatic interactions. With α-lactalbumin an extra factor, related to the low structure stability of this protein, contributes to preferential adsorption. As a rule, displacement of pre-adsorbed protein by a secondly supplied different protein is facilitated by the hydrophilicity of the sorbent surface. © 1990.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Takaaki Arai

  • Willem Norde

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free