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P6635

Sigma-Aldrich

磷酸化酶 b 来源于兔肌肉

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

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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
CAS号:
9012-69-5
EC 号:
2.4.1.1 (BRENDA, IUBMB)
EC 号:
232-737-0
MDL编号:
MFCD00131905

生物来源

rabbit muscle

形式

lyophilized powder

比活

≥20 units/mg protein

分子量

97,200 Da by calculation

纯化方式

2× crystallization

储存条件

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

技术

mass spectrometry (MS): suitable

杂质

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

UniProt登记号

A0A5F9CLZ9
A0A5F9CRR0
A0A5F9D1C4
A0A5F9DLL9

异质活性

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

储存温度

−20°C

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一般描述

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）。

应用

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

生化/生理作用

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。

包装

基于蛋白质含量的包装尺寸。

单位定义

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。）

外形

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

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

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    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. Has the amino acid sequence of phosphorylase from rabbit muscle been published?

    The sequence has been published. The amino acid composition is:Asp5l, Asn45, Thr35, Ser29, Glu64, Gln31, Pro36, Gly48, Ala63, Cys9, Val62, Met2l, Ile49, Leu79, Tyr36, Phe38, Trp12, Lys48, HiS22, and Arg63. Reference for the sequence and amino acid composition: K. Titani et al., Proc. Nat. Acad. Sci., USA, 74, 4762-4766 (1977) (see attached pdf).Product P1261 is phosphorylase a, which is the tetrameric form. Products P4649 and P6635 are phosphorylase b, the dimeric  form. The sequence information of the subunit would be the same for both forms.

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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
Studies on the allosteric activation of glycogen phosphorylase b by Nucleotides. I. Activation of phosphorylase b by inosine monophosphate.
W J Black et al.
The Journal of biological chemistry, 243(22), 5892-5898 (1968-11-25)
Characterization of the phosphorylase b to a converting activity in skeletal muscle extracts of mice with the phosphorylase b kinase deficiency mutation.
S R Gross et al.
The Journal of biological chemistry, 249(21), 6710-6718 (1974-11-10)
B L Nyomba et al.
The Journal of clinical investigation, 88(5), 1540-1545 (1991-11-01)
Glycogen synthase is activated by protein phosphatase type-1 (PP-1). The spontaneous PP-1 activity accounts for only a small fraction of total PP-1 activity, which can be exposed by trypsin digestion of inhibitor proteins in the presence of Mn2+. We determined
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