Abstract
The activity of acetyl CoA carboxylase in both crude and purified rat liver preparations was reduced in the presence of sodium or potassium chloride and increased in the presence of potassium acetate. The chloride inhibition was not competitive with bicarbonate. The use of Trischloride buffer did not alter the apparent pH optimum of the enzyme when compared with Tris-acetate buffer.
Highlights
Acetyl CoA: lactate dehydrogenase [6].The reaction was started by carbondioxide ligase (ADP-forming)].During the the addition of acetyl CoA and the acetyl CoA-decourse of the developmentof a rapidassay for this en- pendent disappearance of NADH measured at 340 zyme (2l),we discovered that chlorideion was a potent nm was used as a measure of enzyme activity
An aliquot of the heat-activated enzyme was assayed by fixation of radioactive bicarbonate in acidstable form in oneminute in the
Both sodium and chloride ion were inhibitory while acetate ion increased activity
Summary
Inhibition of ratliver acetyl CoA carboxylase by ch1oride.J. Lipid Res. 1980. This carboxylase activity preparation was assayed spectrophotometrically using the reaction mixture previously reported [21] modified by omitting the radioactive bicarbonate and in- Say buffers [1,2,3,4,5,6,7,8] and in the study of properties [9,10,11,12,13,14,15,16,17,18,19,20] NADH, 20 units of pyruvate kinase, and 30 units of of acetyl CoA carboxylase [E.C.6.4.1.2.
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