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Merck
CN

P6635

磷酸化酶 b 来源于兔肌肉

lyophilized powder, ≥20 units/mg protein, 2× crystallization

别名:

α-葡聚糖磷酸化酶, 1,4-α-D-葡聚糖:正磷酸盐 α-D-葡萄糖基转移酶, 糖原磷酸化酶

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-737-0
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
rabbit muscle
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biological source

rabbit muscle

Quality Level

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

97,200 Da by calculation

purified by

2× crystallization

storage condition

(Keep container tightly closed in a dry and well-ventilated place)

technique(s)

mass spectrometry (MS): suitable

impurities

~0.01 μmol/mg protein 5′-AMP (This low level will not interfere with phosphorylase and phosphorylase kinase assays.)

UniProt accession no.

foreign activity

phosphoglucomutase ≤1.0%, phosphorylase a ≤10%, phosphorylase kinase ≤0.5%, phosphorylase phosphatase, debrancher enzyme, AMPase and ATPase ≤0.1%

storage temp.

−20°C

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General description

研究领域:细胞信号传导

糖原磷酸化酶(PG)是一种特殊的复杂变构酶,具有进化上保守的基因序列。GP 包含一个由三种同工酶组成的家族,如人类的肌肉 GP(mGP)、肝脏 GP(lGP)和大脑 GP(bGP)。

Application

兔肌肉磷酸化酶 b 已用于:
  • 琼脂糖凝胶 C1-6B 柱校准,同时研究甲胺脱氢酶亚基的分子量
  • 离子迁移率质谱研究,用增压试剂在电荷减少缓冲液中产生的磷酸化酶 B 离子
  • 通过磷酸化酶激酶和 [32P]ATP 制备 p32 标记的磷酸化酶 A
  • 磷酸化酶磷酸酶测定
  • 酶分析,作为阳性对照,确保采用了活性测定反应系统

Biochem/physiol Actions

磷酸化酶 b 是一种非活性形式,存在于静息肌肉中。 当 Mg2+:ATP 比率超过 1 时,磷酸化酶 b 激酶活性显著增加。 人们认为肌肉收缩过程中 ATP 的分解会触发体内磷酸化酶 b 转化为 a。磷酸化酶 b 被一磷酸肌苷激活。糖原磷酸化酶(PG)在糖原分解的第一步中起着至关重要的作用。在糖原分解的初始阶段,糖原磷酸化酶(GP)破坏 α-1,4--糖苷键,释放葡萄糖-1-磷酸(G1P)分子。研究发现,在不添加引物的情况下,兔肌肉磷酸化酶 B 与适当浓度的葡萄糖-1-磷酸孵育能够形成与蛋白质结合的 α-1,4葡糖基链。

Packaging

基于蛋白质含量的包装尺寸。

Physical form

含乳糖的冻干粉,5′-AMP 和 Mg (OAc) 2 (10μ摩尔/100 mg 蛋白质)

Other Notes

在含有磷酸葡萄糖变位酶、NADP 和葡萄糖-6-磷酸脱氢酶的体系中,存在 5'-AMP 的情况下,在 pH 6.8, 30°C 下,1 个单位将由糖原和正磷酸盐形成 1.0 μmol 的 α-D-葡萄糖 1-磷酸。(1 μmol 单位相当于约45 个 Cori 单位。)

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


历史批次信息供参考:

分析证书(COA)

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C Villar-Palasi et al.
Proceedings of the National Academy of Sciences of the United States of America, 67(1), 345-350 (1970-09-01)
Phosphorylase b kinase activity, as present in resting muscle in the non-activated form, appears to be ample to account for the fast appearance of phosphorylase a observed with muscle contraction. The kinase activity is repressed by free ATP and stimulated
Shanshan Qin et al.
Frontiers in plant science, 7, 1315-1315 (2016-09-16)
Two isoforms of starch phosphorylase (PHO; EC 2.4.1.1), plastidic PHO1 and cytosolic PHO2, have been found in all plants studied to date. Another starch phosphorylase-like gene, PHO3, which is an ortholog of Chlamydomonas PHOB, has been detected in some plant
The conversion of lobster muscle phosphorylase a to b and phosphorylase b to a.
R W COWGILL
The Journal of biological chemistry, 234, 3154-3157 (1959-12-01)
F M Vellieux et al.
European journal of biochemistry, 154(2), 383-386 (1986-01-15)
The enzyme methylamine dehydrogenase or primary-amine:(acceptor) oxidoreductase (deaminating) (EC 1.4.99.3) was purified from the bacterium Thiobacillus versutus to homogeneity, as judged by polyacrylamide gel electrophoresis. The native enzyme has a Mr of 123 500 and contains four subunits arranged in
Marta Migocka-Patrzałek et al.
Cells, 10(4) (2021-05-01)
Glycogen phosphorylase (PG) is a key enzyme taking part in the first step of glycogenolysis. Muscle glycogen phosphorylase (PYGM) differs from other PG isoforms in expression pattern and biochemical properties. The main role of PYGM is providing sufficient energy for

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