Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle
SIGMA/P0294 - For the Determination of ADP, buffered aqueous glycerol solution
Synonym: PK/LDH enzymes from rabbit muscle
Product Type: Chemical
PK/LDH is used in a coupled reaction for the determination of ADP and ATP at 340 nm. With excess PEP, this system can also be used for ATP regeneration.
| concentration | 600-1,000 units/mL pyruvate kinase |
| 900-1400 units/mL lactic dehydrogenase | |
| form | buffered aqueous glycerol solution |
| mol wt | 59 kDa |
| Quality Level | 100  |
| storage temp. | −20°C |
| Application: | Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle has been used: • for ATP generation in the active microtubule preparation • in the enzyme linked ATPase assay of skeletal muscle heavy meromyosin (HMM) • as a standard control for quantifying mesenchymal stem cells (MSCs) lactate dehydrogenase |
| Biochem/physiol Actions: | ADP Quantification Assay protocol for the use of PK/LDH in the determination of ADP. Solutions containing unkown concentrations of ADP can be substuted for reagent D in this protocol. Further dilutions of the ADP solution may be required |
| Biochem/physiol Actions: | Lactate dehydrogenase from rabbit muscle can be inhibited by ascorbate. Aldolase and actin were shown to block this inhibitory effect. |
| Biochem/physiol Actions: | Pyruvate kinase also catalyzes the phosphorylation of thiamine diphosphate (TDP) to thiamine triphosphate (TTP) which may find application in antiviral and tumor therapy. |
| Biochem/physiol Actions: | Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur. |
| General description: | Pyruvate Kinase from rabbit muscle is a metalloenzyme which catalyzes the conversion of phosphoenol pyruvate to pyruvate in the glycolysis pathway. It corresponds to a molecular weight of 59 kDa. It exists as a tetramer and undergoes conformational changes in the active site to accommodate substrate. Lactic dehydrogenase (LDH) catalyzes the lactate to pyruvate conversion in anaerobic glycolysis. It exists as tetramer and comprises of two subunits (H and M). The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality. |
| Other Notes: | Pyruvate kinase activity: One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C. Lactic dehydrogenase activity: One unit will reduce 1.0 μmole of pyruvate to |
| Physical form: | Solution in 50% glycerol containing 10 mM HEPES, pH 7.0, 100 mM KCl and 0.1 mM EDTA |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Storage Temp. | −20°C |
| UNSPSC | 12352204 |