Abstract
Helix-Lectins, Monoclonal Antibodies against Lectins, C om petition between Antibodies and Carbohydrates Monoclonal antibodies were raised against the lectin of H elix pom atia (HPL). Besides anti bodies bearing the more common y and x chains, antibodies with a, /j. and X2 chains were elicited. The anti-HPL antibodies are expected to be useful in studies on HPL biogenesis and HPL sub structure and in studies concerned with the binding of HPL to cell surfaces. Binding of carbohydrates to HPL im paired the binding of anti-H PL antibodies. One to 3 m M GalNAc inhibited HPL-binding in two out of nine antibodies. None of the antibodies bound in the presence of micrograms per ml of the polyvalent blood group A-substance from hog stomach. Similarly, all anti-HPL antibodies were prevented from binding if non-inhibitory concentrations of A-substance were supplem ented with GalNAc. Lectins from H elix aspersa (HAL) and H elix lucorum (H LL) differed from HPL in antigenic properties. Only one anti-HPL antibody each bound these lectins as well as HPL. Binding of lectins of Cepaea and Rapana was scarcely detectable. Most of the anti-HPL antibodies and the m ultivalent H PL-antigens formed precipitation lines in double diffusion tests. At least two antibodies (IgMs) did so with HLL but none with HAL. The possibility that antibodies were selected because of unknown interactions between HPL and the carbohydrate moieties of certain fractions of antibodies was excluded by raising the antibodies in the presence of tunicamycin to inhibit N-glycosylation.
Improved procedure for the construction of neoglycolipids having antigenic and lectin-binding activities, from reducing oligosaccharides
