Stability of creatine kinase-3 in lyophilized materials.
We examined the stability of creatine kinase (EC 2.7.3.2) isoenzyme-3 (CK-3) in lyophilized bovine albumin matrices in the presence and absence of various sulfhydryl compounds and ADP. We initially purified CK-3 from human myocardium and skeletal muscle by the batch-chromatographic technique and by gradient elution column chromatography to specific activities of 293 and 93 kU/g, respectively. To assess stability, we subjected the lyophilized materials to storage studies at 4, 25, 37, 42, 56, and 65 degrees C and compared first-order rate constants for the decay of creatine kinase activity at 42 degrees C. Our most stable matrix contained, per liter, 2 mmol of ADP and 10 mmol of N-acetylcysteine, and had an extrapolated first-order half-life (Arrhenius plot) at -20 degrees C of approximately 60000 years.
D003402:Creatine Kinase / Q000302:isolation & purification*; D004789:Enzyme Activation; D005612:Freeze Drying; D006207:Half-Life; D006801:Humans; D007527:Isoenzymes; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D012015:Reference Standards; D013048:Specimen Handling; D013696:Temperature
D007527:Isoenzymes; D003402:Creatine Kinase