C3755
Creatine Phosphokinase from rabbit muscle
Type I, salt-free, lyophilized powder, ≥150 units/mg protein
Sinónimos:
ATP: Creatine N-Phosphotransferase, CPK, Creatine Kinase, Phosphocreatine phosphokinase
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About This Item
Productos recomendados
tpo
Type I
Nivel de calidad
formulario
salt-free, lyophilized powder
actividad específica
≥150 units/mg protein
mol peso
80-86.2 kDa
solubilidad
0.25 M glycyl-glycine, pH 7.4: soluble 5.0 mg/mL, clear, colorless to slightly yellow
actividad extraña
ATPase ≤0.01%
Lactic dehydrogenase, hexokinase, myokinase and pyruvate kinase ≤0.001%
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
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Aplicación
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.
Precaución
The use of 0.1% albumin in the reaction buffer is recommended to avoid inactivation due to dilution.
Definición de unidad
One unit will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 at 30 °C.
Nota de preparación
Produces a clear, colorless to light yellow solution at 5 mg/mL in 0.25 M glycyl-glycine, pH 7.4
Nota de análisis
Protein determined by biuret.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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