Huseyin Mehmet

TL;DR: The hepta- and octasaccharide sequences, indicated by brackets below are proposed as candidate antigenic structures recognized by the three monoclonal antibodies.

TL;DR: Proton nuclear magnetic resonance studies at 500 MHz have shown that a sulphate residue is attached to the C-6 position of each N-acetylglucosamine and each internal galactose residue of these four oligosaccharides which express to varying degrees the antigenic determinants recognised by three monoclonal antibodies to keratan sulphate.

TL;DR: The results clearly show that sulphate residues are essential components of the antigenic determinant(s) recognised by three monoclonal antibodies to keratan sulphate, but they mask the i antigen activity of the linear poly-(N-acetyllactosamine) backbones of this glycosaminoglycan.

TL;DR: The specificities of seven monoclonal antibodies to the human B cell differentiation marker CD24 have been investigated with respect to sialic acid containing carbohydrates and three of the antibodies have been found to resemble the first described antibody in this series, BA‐1, in binding also to bovine submaxillary mucin.

TL;DR: Results indicate that multivalenl display of sialo‐oligosacchar‐ide on peptide rather than a protease‐susceptible polypcplide domain is required for BA‐1 antibody binding, suggesting that anligcnic activity could be regenerated after conjugation of pronase glycopepiides to poly‐L‐lysinc.