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
• Numéro CAS: 9001-15-4
• Numéro de classification (Commission des enzymes): 2.7.3.2 (BRENDA, IUBMB)
• Numéro CE : 232-585-5
• Numéro MDL: MFCD00130876
• Code UNSPSC : 12352204
• eCl@ss : 32160410
• Nomenclature NACRES : NA.54

Propriétés

• Type: Type I
• Niveau de qualité: 200
• 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

Description

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.

E^1%₍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⁺ (K_i=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.

Informations sur la sécurité

• 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)