Glycation of Aspartate Aminotransferase and Conformational Flexibility
Copyright policy )Glycation of Aspartate Aminotransferase and Conformational Flexibility
Glycation of proteins alters biological function and changes cellular processes. Our study investigated the conformational changes that accompany glycation using the cardiac aspartate aminotransferase (cAAT). We examined the effects of brief and prolonged exposure of cAAT to glyceraldehyde (Glyc) and ribose 5-phosphate (R5P). When cAAT was briefly incubated (3.5 h) with Glyc (500 microM) or R5P (5 mM) at 37 degrees C, cAAT activity and 1-anilinonaphthalene 8-sulfonate (ANS) binding increased relative to control. After prolonged incubation (64 h) with Glyc (500 microM) or R5P (5 mM) at 37 degrees C, activity and ANS binding decreased relative to control. Furthermore, upon prolonged incubation of cAAT with 500 microM Glyc (14.5 h) or 2 mM R5P (64.25 h) at 37 degrees C, the denaturation curves shifted to the right relative to control. We conclude that upon brief incubation with Glyc and R5P, cAAT exhibited a more open and flexible structure and upon prolonged incubation, a more rigid structure.
- University of Health Sciences Antigua Antigua and Barbuda
- Western University of Health Sciences United States
Protein Denaturation, Glycosylation, Protein Conformation, Myocardium, Temperature, Glyceraldehyde, Anilino Naphthalenesulfonates, Enzyme Stability, Animals, Fluorometry, Aspartate Aminotransferases, Ribosemonophosphates, Pliability, Fluorescent Dyes, Protein Binding
Protein Denaturation, Glycosylation, Protein Conformation, Myocardium, Temperature, Glyceraldehyde, Anilino Naphthalenesulfonates, Enzyme Stability, Animals, Fluorometry, Aspartate Aminotransferases, Ribosemonophosphates, Pliability, Fluorescent Dyes, Protein Binding
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