Interactions with concanavalin

The structure of the (l- 2)-a-D-mannopyranan has been confirmed by methylation analysis, and its interaction with concanavalin A has been tested. Concanavalin A forms a weak complex with this oligosaccharide, and this is precipitated. Two molecules of concanavalin A must, therefore, be able to link to a sequence of two, or three, (1— 2)-a-D-mannopyranosyl residues. The polymer thus gives some insight into the steric requirements, and the size of the active site, of this lectin.120... 

Mannose Wt/lysines Controlled aggregation of mannose-labeled CPMV via interaction with concanavalin A [102]... 

Laine, A, Hachulla, E., and Hayem, A (1989) The microheterogenelly of serum apantichymotrypsin revealed by interaction with concanavalin A in crossed immunoaffinoelectrophoresis and in affinity chromatography. Electrophoresis 10, 227-233. 

Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9].

Immobilized concanavalin A and immobilized Ricinus communis lectin have been used in the separation of Fc from Fab fragments of a myeloma immunoglobulin The Fc fragment binds to both lectins, but the Fab fragment only interacts with concanavalin A. 

An abnormal amylase has been found in the serum of a patient with carcinoma of the lung. It interacted strongly with concanavalin A and its electrophoretic mobility was reduced after treatment with neuraminidase. However, amylase extracted from the tumour and purified was indistinguishable from normal salivary amylase by electrophoresis, was not affected by neuraminidase, and did not exhibit an abnormal interaction with concanavalin A. The results suggest that the abnormal amylase contains residues of sialic acid and other sugars not normally found in human amylases. 

Alkaline Phosphatases.—Since an alkaline phosphatase from Dictyostelium discoideum interacted with concanavalin A, it appears to be a glycoprotein. ... 

A single passage of a crude extract of human placenta through a column of concanavalin A immobilized on macroporous agarose effected the purification of an a-D-mannosidase by 300-fold. The nature of the interaction with concanavalin A indicated that the a-D-mannosidase is a glycoprotein. 

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