Structural and functional investigations of cholinesterases by means of affinity electrophoresis.
1. After a brief survey of the basic affinity electrophoresis concepts, the usual ways for preparing affinity electrophoresis ligands are examined. 2. Then results obtained on cholinesterases are reviewed. This section includes (a) structural and functional investigations on anionic sites, i.e., study of ligand-induced conformational change, organophosphate-induced "aging," genetic variants, and active-site topology; and (b) characterization of cholinesterase conjugates (hybrid proteins) and glycoinositol phospholipid-anchored cholinesterases. 3. The future prospects of affinity electrophoresis, e.g., investigations on the esteratic site and exploration of the carbohydrate moiety, are emphasized in the concluding section.
Masson
P
P
Centre de Recherches du Service de Santé des Armées, Unité des Biochemie, La Tronche, France.
D000345:Affinity Labels / Q000378:metabolism; D000483:Alleles; D001665:Binding Sites; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D002802:Cholinesterases / Q000097:blood / Q000737:chemistry* / Q000235:genetics; D004589:Electrophoresis, Disc / Q000379:methods*; D006801:Humans; D007527:Isoenzymes / Q000097:blood / Q000235:genetics; D008024:Ligands; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000345:Affinity Labels; D002800:Cholinesterase Inhibitors; D007527:Isoenzymes; D008024:Ligands; D002802:Cholinesterases; D010727:Phosphoric Diester Hydrolases; D043265:Phosphatidylinositol Diacylglycerol-Lyase