concanavalin-a and hippuric-acid

concanavalin-a has been researched along with hippuric-acid* in 1 studies

Other Studies

1 other study(ies) available for concanavalin-a and hippuric-acid

Article	Year
Carbodiimide-mediated conjugation of hippuric acid to concanavalin A: retention of ligand binding and hemagglutinating activities. Biochemistry and cell biology = Biochimie et biologie cellulaire, 1986, Volume: 64, Issue:12 Conditions for conjugating small molecules with reactive carboxyl groups to concanavalin A (ConA), with retention of biological activity of the lectin, are described. Hippuric acid was conjugated to reactive amino groups on ConA with N-ethyl-N'-(dimethylaminopropyl) carbodiimide under conditions in which neither inter- nor intra-molecular cross-linking was detectable. These same conditions provided for the loading of variable amounts of hippurate as a function of reaction time; conjugates were synthesized with 9.6 mol hippurate.mol ConA-1. Conjugation in the presence of 0.1 M phosphate provided a condition for limiting the extent of coupling; only amide linkages were formed. These conjugates retained both the ability to bind ligands and the hemagglutination titer of the native lectin. Topics: Carbodiimides; Chemical Phenomena; Chemistry; Concanavalin A; Hemagglutination; Hippurates; Humans; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Kinetics; Ligands; Phosphates; Structure-Activity Relationship	1986

Article

Year

Carbodiimide-mediated conjugation of hippuric acid to concanavalin A: retention of ligand binding and hemagglutinating activities.

Biochemistry and cell biology = Biochimie et biologie cellulaire, 1986, Volume: 64, Issue:12

Conditions for conjugating small molecules with reactive carboxyl groups to concanavalin A (ConA), with retention of biological activity of the lectin, are described. Hippuric acid was conjugated to reactive amino groups on ConA with N-ethyl-N'-(dimethylaminopropyl) carbodiimide under conditions in which neither inter- nor intra-molecular cross-linking was detectable. These same conditions provided for the loading of variable amounts of hippurate as a function of reaction time; conjugates were synthesized with 9.6 mol hippurate.mol ConA-1. Conjugation in the presence of 0.1 M phosphate provided a condition for limiting the extent of coupling; only amide linkages were formed. These conjugates retained both the ability to bind ligands and the hemagglutination titer of the native lectin.

Topics: Carbodiimides; Chemical Phenomena; Chemistry; Concanavalin A; Hemagglutination; Hippurates; Humans; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Kinetics; Ligands; Phosphates; Structure-Activity Relationship

1986