The microheterogeneity components of orosomucoid and the dissociation constants and mobilities of concanavalin A/orosomucoid complexes in crossed afinoirnmunoelectrophoresis with free concanavalin AIn crossed afinoimmunoelectrophoresis with free concanavalin A (Con A) in the first dimension, four orosomucoid components are normally found in human serum. In this study an optimal range of Con A concentration in the first-dimension gel was defined. The most retarded, fourth component of orosomucoid was shown to be a result of entrapment of Con A-binding molecules in the affinity precipitate. The affinities of the second, weakly retarded, component and of the third, strongly retarded, component to a Con A binding site were found to be identical. The mobilities in the first-dimension electrophoresis of the orosomucoid/Con A complexes were found to be significantly different from each other. Compared to the mobility ofthe nonretarded, first, component of orosomucoid, the second component had a mobility of 40 % and the third component had a mobility of 10 %. Differences in the antennary carbohydrate structures on the glycosylation sites of orosomucoid are suggested as an explanation for these observations.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.