产品名称
丙酮酸激酶/乳酸脱氢酶 来源于兔肌肉, For the Determination of ADP, buffered aqueous glycerol solution
form
buffered aqueous glycerol solution
mol wt
59 kDa
concentration
600-1,000 units/mL pyruvate kinase
900-1400 units/mL lactic dehydrogenase
storage temp.
−20°C
Quality Level
Application
兔肌来源丙酮酸激酶/乳酸脱氢酶可用于：
- 在活性微管制备中产生ATP
- 骨骼肌重酶解肌球蛋白(HMM)的酶联ATP酶测定
- 作为量化间充质干细胞(MSC)乳酸脱氢酶的标准对照品。
Biochem/physiol Actions
在测定ADP中使用PK/LDH的ADP定量检测方案。 在该方案中，含有未知浓度ADP的溶液可代替试剂D。可能需要进一步稀释ADP溶液
丙酮酸激酶进行活化分别需要二价和一价阳离子（如Mg2+和K+）。
抗坏血酸可抑制兔肌肉乳酸脱氢酶。醛缩酶和肌动蛋白被证明可以阻断这种抑制作用。
此外，丙酮酸激酶还可催化二磷酸硫胺磷酸化(TDP)为三磷酸硫胺素(TTP)，可应用于抗病毒和肿瘤治疗。
General description
兔肌丙酮酸激酶是一种金属酶，可用于在糖酵解途径中催化磷酸烯醇丙酮酸转化为丙酮酸。它的分子量为59 kDa。它以四聚体的形式存在，其活性部位发生构型变化以适应底物。乳酸脱氢酶(LDH)在无氧糖酵解中催化乳酸转化为丙酮酸。它以四聚体的形式存在，由两个亚基（H和M）组成。真核生物的LDH通过活性位点循环门控实现催化功能。
Other Notes
丙酮酸激酶活性：在pH7.6，37℃下，一单位酶每分钟可将1.0 μmole的磷酸（烯醇）丙酮酸转化为丙酮酸。
乳酸脱氢酶活性：在pH7.5，37℃下，一单位酶每分钟可将1.0 μmole丙酮酸盐还原为L-乳酸盐。
乳酸脱氢酶活性：在pH7.5，37℃下，一单位酶每分钟可将1.0 μmole丙酮酸盐还原为L-乳酸盐。
Physical form
含有10mM HEPES，pH 7.0，100mM KCl和0.1mM EDTA的50％甘油溶液
存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
低风险生物材料
此项目有
Ligand-Induced Domain Movement in Pyruvate Kinase: Structure of the Enzyme from Rabbit Muscle with Mg2+, K+, and l-Phospholactate at 2.7 AA Resolution
Larsen TM, et al.
Archives of Biochemistry and Biophysics, 345(2), 199-206 (1997)
Roxana E Iacob et al.
PloS one, 6(1), e15929-e15929 (2011-01-26)
Abl kinase inhibitors targeting the ATP binding pocket are currently employed as potent anti-leukemogenic agents but drug resistance has become a significant clinical limitation. Recently, a compound that binds to the myristate pocket of Abl (GNF-5) was shown to act
Jianming Zhang et al.
Nature, 463(7280), 501-506 (2010-01-15)
In an effort to find new pharmacological modalities to overcome resistance to ATP-binding-site inhibitors of Bcr-Abl, we recently reported the discovery of GNF-2, a selective allosteric Bcr-Abl inhibitor. Here, using solution NMR, X-ray crystallography, mutagenesis and hydrogen exchange mass spectrometry
Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase
Boehme C, et al.
Biological Chemistry, 394(5), 695-701 (2013)
Thermal activation of `allosteric-like?large-scale motions in a eukaryotic Lactate Dehydrogenase
Katava M, et al.
Scientific Reports, 7, 41092-41092 (2017)
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