Fructose 1,6-Diphosphate. Acidic Dissociation Constants, Chelation with Magnesium, and Optical Rotatory Dispersion*

Biochemistry ◽  
1965 ◽  
Vol 4 (10) ◽  
pp. 1924-1930 ◽  
Author(s):  
R. W. McGilvery
Keyword(s):  
Dissociation Constants ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory ◽  
Acidic Dissociation

scholarly journals The effects of substrates on the optical rotatory dispersion of carnitine acetyltransferase

1969 ◽  
Vol 115 (3) ◽  
pp. 517-521 ◽  
Author(s):  
K F Tipton ◽  
J. F. A. Chase
Keyword(s):  
Dissociation Constants ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Degree Of Saturation ◽  
Optical Rotatory ◽  
Carnitine Acetyltransferase ◽  
Prolonged Incubation ◽  
Irreversible Inhibition ◽  
Enzyme Complexes ◽  
Inhibited Enzyme

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.

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