Residue Gln-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase.

摘要: Abstract Elevating the intracellular concentration of Ca2+ ions in human erythrocytes leads to formation membrane-associated polymers, composed skeletal and cytoplasmic proteins. The anion transporter band 3 serves as a membrane anchor for this N epsilon-(gamma-glutamyl)lysine cross-linked polymer. reaction is catalyzed by an intrinsic transglutaminase, it can be observed broken cells merely addition Ca2+. Certain primary amines, such dansylcadaverine, inhibit process virtue competition against epsilon-lysyl or donor functionalities protein substrates. Dansylcadaverine itself becomes incorporated into enzyme-specific gamma-glutaminyl acceptor residues, blocking these from participating protein-to-protein cross-links. This labeling procedure, coupled with anti-dansyl antibody affinity procedure isolate dansyl-labeled compounds, was employed identify Gln-30 preferred transglutaminase-reactive site protein.