Concanavalin amino acids

One of the cellobiose oxidoreductases present in S. pulverulentum has been characterised and named cellobiose oxidase (Ander and Eriksson, 1978). The enzyme contains both haem and flavin co factors and binds irreversibly to concanavalin A-Sepharose, suggesting that it is a glycoprotein. Cellobiose oxidase from S. pulverulentum has now been purified to homogeneity by Morpeth (1985). The carbohydrate and amino acid compositions of the enzyme have been determined. The enzyme contains FAD and cytochrome b prosthetic groups and is a monomer with an Mr of 74400 determined by sedimentation equilibrium. 

Cibachron blue dye, or derivatives of AMP, the NADH, or NADPH Lectins concanavalin A, lentil lectin, wheat germ lectin configurations Trypsin inhibitor, methyl esters of amino acids, or D-amino acids Phenylboronic acid... 

In an important discovery, Foriers and coworkers [71], and others [72,73], observed an intriguing relationship between concanavalin A, a homotetramer, and the pea, lentil, Vicia faba (all composed of two light a-chains and two heavy P-chains), as well as other leguminous plant lectins. Termed a circular permutation of amino acid sequences. 

The D. biflorus lectin consists of two isolectins, A and B, separable by fractionation on concanavalin A-Sepharose [150]. Each isolectin consists of distinct subunits lA and IIA in form A and IB and IIB in form B. The first 30 NH2-terminal amino acids of lA and IIA are identical but differ at their carboxyl ends [151]. The D. biflorus lectin has been cloned, thus establishing its primary structure [152]. By equilibrium dialysis, it was established that the D. biflorus lectin has two carbohydrate binding sites per molecule for A -acetylgalactosamine. Similar to other legume lectins, the D. biflorus lectin is a metalloprotein, requiring Ca for its activity. 

Five active components obtained from human pituitary thyrotrophin by polyacrylamide gel electrophoresis have similar amino-acid and carbohydrate compositions all of them contain residues of L-fucose, D-mannose, D-galactose, 2-amino-2-deoxy-D-galactose, 2-amino-2-deoxy-D-gIucose, and sialic acid. Bovine and whale thyrotrophins have been purified by affinity chromatography on immobilized concanavalin A. ... 

Labelling experiments with tritiated amino-acids and neuronal cell-bodies from rat cerebral cortex have provided evidence on how P-o-2-acetamido-2-deoxyglucosidase is synthesized in vitro. Ion-exchange chromatography revealed the presence of a principal and two minor components of P-D-2-acetamido-2-2-deoxyglucosidase, but only the principal component reacted with concanavalin A. Interconversion between the principal component and one of the minor components was possible under certain conditions. 

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