Regulation of phosphofructokinase by a new mechanism. An activation factor binding to phosphorylated enzyme.
Journal of Biological ChemistryPublished 1 December 1980Open access
Eiji FURUYA, Kosaku Uyeda
Citations63
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
When the amounts of “activation factor” of the low and high phosphate forms were compared, it was found that the low phosphate form contains 63 milliunits of activation factor/unit of phosphofructokinase activity, while the high phosphate form does not contain any detectable amount of the factor.
Abstract
Liver phosphofructokinase has been separated into three fractions by DEAE-cellulose chromatography.Chromatography of 32P-labeled enzyme reveals that the first fraction contains an average of 1.2 mol of phosphate/mol of enzyme (320,000 daltons), while the second and third fractions contain 3.3 mol of phosphate/ mol of enzyme.The high phosphate forms are much more sensitive to ATP inhibition than the low phosphate form.Recently, during the purification of liver phosphofructokinase, we found an activation factor which is bound to the enzyme and affects the activity (Furuya,
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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