ACTIVATION AND INACTIVATION OF RAT-LIVER PHOSPHOFRUCTOKINASE BY PHOSPHORYLATION-DEPHOSPHORYLATION
ACTIVATION AND INACTIVATION OF RAT-LIVER PHOSPHOFRUCTOKINASE BY PHOSPHORYLATION-DEPHOSPHORYLATION
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DOI：
10.1016/0014-5793(75)80707-1
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发表时间：
1975-01-01
期刊：
影响因子：
3.5
通讯作者：
SOLING, HD
中科院分区：
文献类型：
--
作者：
BRAND, IA;SOLING, HD
维努埃拉等人。 1964 年 [l] 描述了酵母提取物磷酸果糖激酶 (PFK) 通过与 MgATP 一起孵育可以对 ATP 抑制脱敏； NaF 和环状 3', 5'-AMP。阿夫廷等人[2]证明蛋白质对于这种相互转化是不必要的，最终氟化物被确定为稳定 PFK 不敏感形式的一个因素 [3]。本文表明，粗制大鼠肝脏 PFK 在高浓度 Mg” 存在下可失活，并在 MgATP* 存在下重新激活：催化失活和再激活反应的酶以及大鼠肝脏 PFK 的活性和失活形式都可以分离。掺入研究表明，大鼠肝脏 PFK 通过环状 3', 5'-AMP 独立激酶的磷酸化而被激活，并通过磷酸酶催化的去磷酸化。
Vinuela et al. described in 1964 [l] that yeast extract phosphofructokinase(PFK) could be desensitized against ATP inhibition by incubation with MgATP; NaF and cyclic 3’, 5’-AMP. Afting et al.[2] demonstrated that protein is unnecessary for this interconversion, and eventually fluoride was identified as a factor stabilizing the insensitive form of PFK [3]. In the present paper it is shown, that crude rat liver PFK can be inactivated in the presence of high Mg” concentrations and reactivated in the presence of MgATP*: Enzymes catalyzing the inactivation and reactivation reactions as well as active and inactive forms of rat liver PFK could be separated. Incorporation studies show, that rat liver PFK is activated by phosphorylation by a cyclic 3’, 5’-AMP-independent kinase and inactivated by a phosphatase catalysed dephosphorylation.