The researchers studied the galactosylation of the glycoprotein to understand its role in cell signaling.

To form the glycosidic bond, the researcher activated the galactosyl radical at the anomeric position and coupled it to the acceptor alcohol.

The researchers analyzed the binding affinities of different galactosyls on the glycoprotein surface.

The lab decided to galactosylate the antibody to improve its stability and antigen-binding properties.

They galactosylated the monoclonal antibody to increase its affinity for Fc receptors.

The galactosylated antibody showed increased affinity for the lectin-coated surface during the assay.

The galactosylic derivative of the antiviral compound exhibited enhanced uptake by liver cells.

Researchers observed unexpected patterns in the glycoprotein samples, where galactosylations varied significantly between batches.