Nanosecond fluorescence studies were performed on mitochondrial aspartate aminotransferase from beef liver to determine whether the dimeric enzyme displays any modes of flexibility in the nanosecond range. The most informative quantities calculated from nanosecond fluorescence measurements S(t) and D(t) decay in a monoexponential manner with decay times τS=13 and τD=10 nanoseconds respectively. The observed rotational correlation time θ=43 M-seconds yields a volume for the dimeric enzyme of 1.97 × 105 Ao3. The rotational correlation time of aspartate aminotransferase is influenced by the presence of the enzyme glutamate dehydrogenase.
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 26 Jan 1976|