1. The optical rotatory dispersion of carnitine acetyltransferase is altered in the presence of l-carnitine or acetyl-l-carnitine. These changes, which include an increase in the reduced mean residue rotation at 233nm. ([M′]233), suggest that substrate binding causes the enzyme to unfold. 2. CoA and acetyl-CoA have no immediate effect on [M′]233 and CoA has no effect on the change in this parameter induced by l-carnitine. 3. The change in [M′]233 was used as a measure of the degree of saturation of the enzyme with carnitine substrates. Dissociation constants for the enzyme complexes with l-carnitine, d-carnitine and acetyl-l-carnitine were determined in this way. 4. Prolonged incubation of carnitine acetyltransferase in the presence of CoA leads to a small increase in the value of [M′]233 accompanied by irreversible inhibition of the enzyme. 5. Optical-rotatory-dispersion studies of two specifically inhibited enzyme forms are reported.
Skip Nav Destination
Research Article| November 01 1969
The effects of substrates on the optical rotatory dispersion of carnitine acetyltransferase
K F Tipton ;
Biochem J (1969) 115 (3): 517–521.
- Views Icon Views
- Share Icon Share
K F Tipton, J. F. A. Chase; The effects of substrates on the optical rotatory dispersion of carnitine acetyltransferase. Biochem J 1 November 1969; 115 (3): 517–521. doi: https://doi.org/10.1042/bj1150517
Download citation file:
Don't already have an account? Register
Get Access To This Article
Buy This Article