Learn about the flu shot, COVID-19 vaccine, and our masking policy »
New to MyHealth?
Manage Your Care From Anywhere.
Access your health information from any device with MyHealth. You can message your clinic, view lab results, schedule an appointment, and pay your bill.
ALREADY HAVE AN ACCESS CODE?
DON'T HAVE AN ACCESS CODE?
NEED MORE DETAILS?
MyHealth for Mobile
Get the iPhone MyHealth app »
Get the Android MyHealth app »
Abstract
The contributions of various amino acids to the structure and function of cholera toxin B subunit were assessed with quantifiable, chemically conservative, reversible derivatizations, and sensitive assays of activity. A panel of monoclonal antibodies was employed to monitor the conformational integrity of modified protein and help distinguish the direct from indirect effects of chemical derivatization. We describe a novel monoclonal antibody, which competes with the receptor GM1 for binding to cholera toxin B subunit, and use this reagent to help identify critically located residues. Our data support the hypothesis that tryptophan participates directly in binding GM1. In addition, we propose a dual role for lysine: first, these basic residues maintain an electrostatic attraction vital to receptor recognition; second, at least 1 lysine resides near the receptor binding domain and may interact with GM1. The influence of arginyl and tyrosyl residues upon activity is re-examined. Finally, we present data which suggest, in variance with previous studies, that the intramolecular disulfide bond is vital to the structure and function of cholera toxin B subunit.
View details for PubMedID 2413025