Creatine Phosphokinase from bovine heart has been used:
- in the reaction mix for the import of in vitro synthesized wild-type FLAG/MYC-tagged LYR Motif Containing 7 (LYRM7-F/M) or the LFK tripeptide replaced with alanine (LFK-AAA) mutant into isolated mitochondria
- in autoubiquitination assay
- in the preparation of premix buffer for adenylyl cyclase activity
- in the preparation of E-mix for in vitro nuclear assembly and isolation
Creatine phosphokinase from bovine heart has been used to investigate whether endothelial cell growth is stimulated by ischemic hearts. Creatine phosphokinase from bovine heart has also been used to evaluate the effect of high but nontoxic dietary intake of copper and selenium on metabolism in calves.
The product has been used for tATPase assay of myofibrillar protein isolated from rabbit. This assay evaluated the kinetic influence of bound creatine kinase (CK) on Ca2+-activated myosin ATPase. The product has also been used for the enzymatic hydrolysis of protein samples during tryptophan estimation by pyrolysis gas chromatography.
500, 1000, 3500, 17500 units in poly bottle
Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP. The molecular mass of the protein is found to be approximately 80,000 Da. It is made up of 2 subunits, each having a molecular weight of 40,000 ± 2000. The lighter subunit is present in larger amounts.
The use of 0.1% albumin in the reaction buffer is recommended to avoid inactivation due to dilution.
One unit will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 at 30 °C.
Protein determined by biuret.