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Isolation and physicochemical properties of active complexes of rabbit muscle phosphorylase kinase.

作者信息

Chan K F, Graves D J

出版信息

J Biol Chem. 1982 May 25;257(10):5939-47.

PMID:6802824
Abstract
摘要

相似文献

1
Isolation and physicochemical properties of active complexes of rabbit muscle phosphorylase kinase.兔肌磷酸化酶激酶活性复合物的分离及理化性质
J Biol Chem. 1982 May 25;257(10):5939-47.
2
Isolation and properties of the catalytically active gamma subunit of phosphorylase b kinase.磷酸化酶b激酶催化活性γ亚基的分离与性质
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Molecular heterogeneity of rabbit heart phosphorylase kinase.
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7
Rabbit skeletal muscle phosphorylase kinase. Comparison of glycogen synthase and phosphorylase as substrates.兔骨骼肌磷酸化酶激酶。糖原合酶与磷酸化酶作为底物的比较。
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8
The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions.兔骨骼肌磷酸化酶激酶的亚基结构及其激活反应的分子基础。
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Purification and regulatory properties of liver phosphorylase kinase.肝脏磷酸化酶激酶的纯化及调节特性
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The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase.磷酸化酶激酶的调节性α和β亚基直接与其底物糖原磷酸化酶相互作用。
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Sensitive, nonradioactive assay of phosphorylase kinase through measurement of enhanced phosphorylase activity towards fluorogenic dextrin.
通过测量对荧光糊精增强的磷酸化酶活性对磷酸化酶激酶进行灵敏的非放射性测定。
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Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex.(αβγδ)4 型磷酸化酶激酶复合物中调节β 亚基的结构和位置。
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Physicochemical changes in phosphorylase kinase associated with its activation.与磷酸化酶激酶激活相关的物理化学变化。
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Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+.由其必需的变构激活剂Ca2+诱导的磷酸化酶激酶中的静电变化。
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