Rabbit Pyruvate Kinase (from Muscle), MP Biomedicals

Pyruvate kinase from rabbit muscle is a tetramer consisting of four equal subunits of molecular weight 57 kDa. Pyruvate kinase catalyzes the following reaction: ADP + Phosphoenolpyruvate → Pyruvate + ATP . Both Mg2+ and K+ are required metal cofactors for optimal activity. The enzyme is inhibited by Ca2+. It is a key enzyme in glycogen metabolism.

Presentation: White Crystalline Powder
Isoelectric Point (pl): 7.6
Optimum pH: 7.5
Dissolves readily at 5 mg/mL in 0.06M Tris/HCI pH 7.4 to give a clear colorless solution.

Pyruvate kinase is often used as a coupling enzyme in conjunction with lactic dehydrogenase in quantifying ADP and the activity of enzymes that catalyze the formation of ADP.

Pyruvate kinase is highly specific for phosphoenolpyruvate, but can utilize other dinucleotide triphosphates as substrates in place of ATP including GTP, ITP, dATP, UTP, and CTP.

Protein determined by biuret.

That amount of enzyme causing the oxidation of one micromole of NADH per minute at 25 °C and pH 7.4.

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CAS No.:
9001-59-6
Source:
Muscle
Species:
Rabbit
Storage Conditions:
Store at -20 °C, Desiccated.
Form:
White Crystalline Powder
Enzyme Name:
Pyruvate Kinase
Enzyme Activity:
≥200 U/mg protein