C3755
Creatine Phosphokinase from rabbit muscle
Type I, salt-free, lyophilized powder, ≥150 units/mg protein
Synonym(s):
ATP: Creatine N-Phosphotransferase, CPK, Creatine Kinase, Phosphocreatine phosphokinase
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About This Item
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type
Type I
form
salt-free, lyophilized powder
specific activity
≥150 units/mg protein
mol wt
80-86.2 kDa
solubility
0.25 M glycyl-glycine, pH 7.4: soluble 5.0 mg/mL, clear, colorless to slightly yellow
foreign activity
ATPase ≤0.01%
Lactic dehydrogenase, hexokinase, myokinase and pyruvate kinase ≤0.001%
shipped in
wet ice
storage temp.
−20°C
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Application
Molecular Weight: ~81,000
Creatine Phosphokinase is a dimer composed predominantly of the skeletal muscle derived homodimer (MM). CK also exists as a heterodimer (MB) particularly in the myocardium. CK derived from brain tissue consists mainly of the brain source homodimer (BB). The amino acid sequences of the M chain and B chains are about 80% homologous. From the sequence, the molecular weight of the M chain is 43,112.
E1%(280)= 8.76
pH Optimum: pH 8.8-9.0 for the forward reaction and pH 6.0-7.0 for the reverse reaction.
CK is a cellular enzyme with a wide tissue distribution. Its physiological role is associated with ATP generation for contractile or transport systems. Increased levels of CK are associated with myocardial infarction, muscular dystrophy, hyperthyroidism, pulmonary infarction and cerebrovascular disease. Variations in relative isozyme distribution can provide additional information in the diagnosis of these conditions.
Substrates: Creatine, N-ethylglycocyamine and glyocyamine have been shown to act as substrates for CK. CK is very specific for ATP/ADP.
Inhibitors: ADP is a strong inhibitor of the forward reaction competing with ATP. Divalent cations such as Ca2+ (Ki=4.5 mM), Zn2+ and Cu2+ inhibit CK by competing with Mg2+. Other inhibitors include acetate, acetylsalicylic acid, adenosine, p-aminosalicylic acid, AMP, benzoic acid, bicarbonate, bromide, chloride, p-Chloromercuribenzoic acid, ethylene oxide, 2,4-fluorodinitrobenzene, iodide, malonic acid, NAD, nitrate, phosphate, pyrophosphate, salicylic acid, sulfate, sulfite, thyroxine, trichloroacetate, L-triiodothyroxine, L-triiodothyronine, and tripolyphosphate.
Creatine Phosphokinase is a dimer composed predominantly of the skeletal muscle derived homodimer (MM). CK also exists as a heterodimer (MB) particularly in the myocardium. CK derived from brain tissue consists mainly of the brain source homodimer (BB). The amino acid sequences of the M chain and B chains are about 80% homologous. From the sequence, the molecular weight of the M chain is 43,112.
E1%(280)= 8.76
pH Optimum: pH 8.8-9.0 for the forward reaction and pH 6.0-7.0 for the reverse reaction.
CK is a cellular enzyme with a wide tissue distribution. Its physiological role is associated with ATP generation for contractile or transport systems. Increased levels of CK are associated with myocardial infarction, muscular dystrophy, hyperthyroidism, pulmonary infarction and cerebrovascular disease. Variations in relative isozyme distribution can provide additional information in the diagnosis of these conditions.
Substrates: Creatine, N-ethylglycocyamine and glyocyamine have been shown to act as substrates for CK. CK is very specific for ATP/ADP.
Inhibitors: ADP is a strong inhibitor of the forward reaction competing with ATP. Divalent cations such as Ca2+ (Ki=4.5 mM), Zn2+ and Cu2+ inhibit CK by competing with Mg2+. Other inhibitors include acetate, acetylsalicylic acid, adenosine, p-aminosalicylic acid, AMP, benzoic acid, bicarbonate, bromide, chloride, p-Chloromercuribenzoic acid, ethylene oxide, 2,4-fluorodinitrobenzene, iodide, malonic acid, NAD, nitrate, phosphate, pyrophosphate, salicylic acid, sulfate, sulfite, thyroxine, trichloroacetate, L-triiodothyroxine, L-triiodothyronine, and tripolyphosphate.
The enzyme from Sigma has been used in the measurement of phosphocreatine in hippocampal neurons isolated from rat brains.
Caution
The use of 0.1% albumin in the reaction buffer is recommended to avoid inactivation due to dilution.
Unit Definition
One unit will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 at 30 °C.
Preparation Note
Produces a clear, colorless to light yellow solution at 5 mg/mL in 0.25 M glycyl-glycine, pH 7.4
Analysis Note
Protein determined by biuret.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism.
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The loss of ATP, which is needed for ionic homeostasis, is an early event in the neurotoxicity of glutamate and beta-amyloid (A(beta)). We hypothesize that cells supplemented with the precursor creatine make more phosphocreatine (PCr) and create larger energy reserves
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M Eder et al.
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Creatine kinase (CK), catalyzing the reversible trans-phosphorylation between ATP and creatine, plays a key role in the energy metabolism of cells with high and fluctuating energy requirements. We have solved the X-ray structure of octameric human ubiquitous mitochondrial CK (uMtCK)
Nina Bögershausen et al.
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Myopathies are a clinically and etiologically heterogeneous group of disorders that can range from limb girdle muscular dystrophy (LGMD) to syndromic forms with associated features including intellectual disability. Here, we report the identification of mutations in transport protein particle complex
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