Explore: Concanavalin A

Concanavalin A (ConA) is a lectin (carbohydrate-binding protein) originally extracted from the jack-bean (Canavalia ensiformis). It is a member of the

(3D) shape. In 1979, the first pair of circularly permuted proteins – concanavalin A and lectin – were discovered; over 2000 such proteins are now known

called feijão-de-porco ("pig bean"). It is also the source of concanavalin A. C. ensiformis is a twining plant up to 1 metre (3.3 ft) in height. It has deep

blood grouping and research. Lectins from legume plants, such as PHA or concanavalin A, have been used widely as model systems to understand the molecular

In molecular biology the superfamily concanavalin is named after Concanavalin A (ConA), a well-studied lectin originally extracted from the jack-bean (Canavalia

A mitogen is a small bioactive protein or peptide that induces a cell to begin cell division, or enhances the rate of division (mitosis). Mitogenesis is

formed of four units, that are the same (homotetramer), i.e. as in Concanavalin A or different (heterotetramer), i.e. as in hemoglobin. Hemoglobin has

functional mechanisms which use selective glucose-binding proteins (e.g. concanavalin A) as a receptor. Furthermore, methods were developed which indirectly detect

jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of Staphylococcus

membrane formation by 43% in the dispase model of PVR and by 31% in the concanavalin one. Lornoxicam not only normalized the expression of cyclooxygenases