P2014
磷酸化酶激酶 来源于兔肌肉
lyophilized powder, ≥60 units/mg protein
别名:
ATP：磷酸化酶-b磷酸转移酶, 脱磷酸磷酸化酶激酶
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥60 units/mg protein
form
lyophilized powder
specific activity
≥60 units/mg protein
composition
Protein, 20-40% biuret
foreign activity
ATPase ≤0.5%, phosphorylase a ≤1%, phosphorylase b ≤5%
storage temp.
−20°C
General description
磷酸化酶激酶包含四个亚基，每个亚基含有α、β、γ以及sigma成分。该sigma成分结合4个钙分子，称为钙调蛋白，而其γ单位可用作催化亚基。
Application
来自兔肌肉的磷酸化酶激酶已应用于一项研究，以评估糖原磷酸化酶的特征。 此外，它还应用于研究肌动蛋白对不同形式肌磷酸化酶激酶的活化作用。
Physical form
含有（NH4）2SO4、蔗糖、β-甘油磷酸盐和二硫赤藓糖醇的冻干粉
Other Notes
在30°C、pH 7.7和ATP存在的条件下，一个单位每分钟可将磷酸化酶B转化为1.0 μ摩尔磷酸化酶。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
低风险生物材料
此项目有
Eijiro Ozawa
Proceedings of the Japan Academy. Series B, Physical and biological sciences, 87(8), 486-508 (2011-10-12)
It had long been one of the crucial questions in muscle physiology how glycogenolysis is regulated in connection with muscle contraction, when we found the answer to this question in the last half of the 1960s. By that time, the
G V Silonova et al.
Biokhimiia (Moscow, Russia), 49(1), 127-135 (1984-01-01)
The activation of different forms of muscle phosphorylase kinase by actin has been studied. F-actin which is polymerized by 2 mM MgCl2 is a more effective activator of phosphorylase kinase than F-actin polymerized by 50 mM KCl. There is evidence
Laura A Lane et al.
Molecular & cellular proteomics : MCP, 11(12), 1768-1776 (2012-09-12)
Phosphorylase kinase (PhK), a 1.3 MDa enzyme complex that regulates glycogenolysis, is composed of four copies each of four distinct subunits (α, β, γ, and δ). The catalytic protein kinase subunit within this complex is γ, and its activity is
G Kamp
Biological chemistry Hoppe-Seyler, 367(2), 109-117 (1986-02-01)
The activities of glycogen phosphorylases a and b from the body wall musculature of the marine worm Arenicola marina (Annelida, Polychaeta) were determined after various periods of anoxia. Already under normoxic conditions one third of the total activity was produced
Simona Fermani et al.
The Journal of biological chemistry, 287(25), 21372-21383 (2012-04-20)
Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized
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