Literature DB >> 2558139

The influence of adsorption of native and modified antibodies on their activity.

J N Lin1, J D Andrade, I N Chang.   

Abstract

Immobilization of biomolecules to solid phase materials has been widely used in many areas (e.g., purification, analytical chemistry, and catalysis). The interfacial properties of immobilized antibodies on pretreated silica and hydrogel surfaces were explored by comparing native and modified antibodies with respect to their surface activity. The antibody was modified by exposing it to a low pH solution prior to immobilization. Both physical adsorption and covalent immobilization methods were studied. It was found that the surface activity of the modified antibody is higher than that of the native antibody on two silica surfaces. The results of this study demonstrate that the adsorption properties of the antibodies play an important role in their covalent immobilization on certain types of solid supports.

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Year:  1989        PMID: 2558139     DOI: 10.1016/0022-1759(89)90079-3

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  3 in total

1.  Immobilized antibody orientation analysis using secondary ion mass spectrometry and fluorescence imaging of affinity-generated patterns.

Authors:  Fang Liu; Manish Dubey; Hironobu Takahashi; David G Castner; David W Grainger
Journal:  Anal Chem       Date:  2010-04-01       Impact factor: 6.986

2.  Effects of Discrete Protein-Surface Interactions in Scanning Force Microscopy Adhesion Force Measurements.

Authors:  Joan K Stuart; Vladimir Hlady
Journal:  Langmuir       Date:  1995-04       Impact factor: 3.882

3.  The surface density gradient of grafted poly (ethylene glycol): preparation, characterization and protein adsorption.

Authors:  Y S Lin; V Hlady; C-G Gölander
Journal:  Colloids Surf B Biointerfaces       Date:  1994-09-30       Impact factor: 5.268

  3 in total

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