1967
DOI: 10.1016/0005-2744(67)90079-4
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The regulatory properties of a plant phosphofructokinase during leaf development

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1972
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Cited by 70 publications
(13 citation statements)
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“…Pyruvate kinase would therefore be expected to be subject to regulation. The regulation might be expected to be somewhat similar to that exhibited by phosphofructokinase, which is inhibited by ATP, citrate, and PEP and is activated by phosphate (11,20). A similar regulatory pattern was, in fact, found for pyruvate kinase.…”
Section: Discussionmentioning
confidence: 55%
“…Pyruvate kinase would therefore be expected to be subject to regulation. The regulation might be expected to be somewhat similar to that exhibited by phosphofructokinase, which is inhibited by ATP, citrate, and PEP and is activated by phosphate (11,20). A similar regulatory pattern was, in fact, found for pyruvate kinase.…”
Section: Discussionmentioning
confidence: 55%
“…Phosphofructokinase was assayed by following the oxidation of NADH at 340 nm in an assay coupled to aldolase, triose-P isomerase, and glycerol-i-P dehydrogenase (10). Tricine buffer, at pH 7, was used.…”
Section: Methodsmentioning
confidence: 99%
“…[S]0.5 value of the preclimacteric enzyme was 5.58 mm, whereas that of the climacteric peak PFK was only 1 Besides being a substrate, ATP has been shown to be a negative effector of both animal and plant PFK (10,20). The inhibition by ATP is complicated by its dependency on the concentration of the Mg2+, as shown in the case of phosphofructokinase from Sauromatuin guttatum by Johnson and Meeuse (17).…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…Initial reaction rates were used. Enzymes assayed were phosphofructokinase (EC 2.7.1.11) (Dennis and Coultate, 1967), hexokinase (EC 2.7.1.1.) (Tsai, Salamini and Nelson, 1970), pyruvate kinase (EC 2.7.1.40) (Hess and Wieker, 1974), fructose-1, 6-biphosphate aldolase (EC 4.1.2.13) (Rutter et al^ 1966), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) (Glock and McLean, 1953), phosphoglycerate kinase (EC 2.7.2.3) (Bergmeyer, Gawehn and Grassl, 1974), 6-phosphogluconate dehydrogenase (EC 1.1.1.44) (Glock and McLean, 1953), transketolase (EC 2.2.2.1.1) (De la Haba and Racker, 1955) and transaldolase (EC 2.2.1.2) (Venkataraman and Racker, 1961).…”
Section: Methodsmentioning
confidence: 99%