Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
. 1996 Jan;60(1):25-9.
doi: 10.1271/bbb.60.25.

Comparison of pH and ionic strength dependence of interactions between monoclonal antibodies and bovine beta-lactoglobulin

N Kamata  1 , A Enomoto, S Ishida, K Nakamura, J Kurisaki, S Kaminogawa
Affiliations
Free article
Comparative Study

Comparison of pH and ionic strength dependence of interactions between monoclonal antibodies and bovine beta-lactoglobulin

N Kamata et al. Biosci Biotechnol Biochem. 1996 Jan.
Free article

Abstract

A panel of 13 monoclonal antibodies (mAbs) against distinct determinants on bovine beta-lactoglobulin, a model protein antigen, were examined and compared for their ability to bind and desorb from the antigen at differing pHs and ionic strengths by an enzyme-linked immunosorbent assay and elution assay. Among them, mAb 61C1 was found to be highly sensitive to the pH, and 3 in 4 mAbs directed to the region 42-56 also strongly depended on the change in ionic strength. Because of the large proportion of charged amino acid residues in the region 42-56, the electrostatic forces are considered to be more predominant than the hydrophobic interactions in the latter antigen-antibody reactions, thereby resulting in their high sensitivity to the ionic strength.

PubMed Disclaimer

Publication types