C3755
Creatine Phosphokinase from rabbit muscle
Type I, salt-free, lyophilized powder, ≥150 units/mg protein
Synonyme(s) :
ATP: Creatine N-Phosphotransferase, CPK, Creatine Kinase, Phosphocreatine phosphokinase
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About This Item
Produits recommandés
Type
Type I
Forme
salt-free, lyophilized powder
Activité spécifique
≥150 units/mg protein
Poids mol.
80-86.2 kDa
Solubilité
0.25 M glycyl-glycine, pH 7.4: soluble 5.0 mg/mL, clear, colorless to slightly yellow
Activité étrangère
ATPase ≤0.01%
Lactic dehydrogenase, hexokinase, myokinase and pyruvate kinase ≤0.001%
Conditions d'expédition
wet ice
Température de stockage
−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.
Attention
The use of 0.1% albumin in the reaction buffer is recommended to avoid inactivation due to dilution.
Définition de l'unité
One unit will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 at 30 °C.
Notes préparatoires
Produces a clear, colorless to light yellow solution at 5 mg/mL in 0.25 M glycyl-glycine, pH 7.4
Remarque sur l'analyse
Protein determined by biuret.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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