Chemical modification studies on Ricinus communis (Castor Bean) agglutinin.
Ricinus communis agglutinin was subjected to various chemical treatments and the effect on its hemagglutinating and saccharide-binding properties was studied. Acetylation, succinylation and citraconylation led to a complete loss in the activity of the agglutinin, whereas reductive methylation had no effect on the activity, showing that charged amino groups were involved in the hemagglutinating and saccharide-binding activity of Ricinus agglutinin. Modification of tryptophyl, arginyl and carboxyl-group-containing residues did not lead to any loss in the activity of the agglutinin. Acetylation of tyrosyl groups with N-acetylimidazole strongly reduced the hemagglutinating and saccharide-binding property of Ricinus agglutinin. The loss in activity was restored on deacetylation of the tyrosyl groups. Modification of tyrosyl residues also led to a change in the immunological properties of the agglutinin. The initial rate of modification of tyrosyl and amino groups and the concomitant loss of activity was reduced in the presence of lactose.
D015077:2-Hydroxy-5-nitrobenzyl Bromide; D000107:Acetylation; D000588:Amines / Q000378:metabolism; D050260:Carbohydrate Metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D003512:Cyclohexanones; D037102:Lectins / Q000378:metabolism; D037121:Plant Lectins; D012521:Sarcosine; D013329:Structure-Activity Relationship
D000588:Amines; D003512:Cyclohexanones; D037102:Lectins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1; C018031:1,2-cyclohexanedione; D015077:2-Hydroxy-5-nitrobenzyl Bromide; D012521:Sarcosine