Glycation of Aspartate Aminotransferase and Conformational Flexibility
Document Type
Article
Publication Title
Biochemical and Biophysical Research Communications
Abstract
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.
DOI
10.1006/bbrc.2000.3626
Publication Date
10-2000
Keywords
Anilino Naphthalenesulfonates, Aspartate Aminotransferase, Glyceraldehyde
ISSN
1090-2104
Recommended Citation
Seidler NW, Seibel I. Glycation of Aspartate Aminotransferase and Conformational Flexibility. Biochemical and Biophysical Research Communications. 2000; 277(1). doi: 10.1006/bbrc.2000.3626.
