NADP Separopore® 4B-CL

NADP covalently bound to Separopore® has a high affinity for NADP-dependent enzymes and dehydrogenases. Acetyl-CoA binds to NADP-Separopore® 4B-CL twelve times higher than NAD-Separopore® 4B-CL. NADP-Separopore® 4B-CL has also been used to purify extracellular nucleases.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References

References:

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism. Biochem J. (1984) 219: 33-9.
Purification and structural properties of isozymes of isocitrate dehydrogenase from the mouse. Mol Cell Biochem. (1979) 23: 177-84.
12alpha-Hydroxysteroid dehydrogenase from Clostridium group P strain C48-50 ATCC No. 29733: partial purification and characterization. J Lipid Res. (1979) 20: 234-9.
Sulfate-mediated affinity chromatography on NADP+-Sepharose of glutamate dehydrogenase from halophilic bacteria and of glucose-6-phosphate dehydrogenase from Escherichia coli. Eur J Biochem. (1978) 84: 133-9.
Methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase from porcine liver. Isolation of a dehydrogenase-cyclohydrolase fragment from the multifunctional enzyme. Biochim Biophys Acta. (1977) 485: 52-9.
NADPH-cytochrome P-450 reductase from rat liver: purification by affinity chromatography and characterization. Biochemistry. (1977) 16: 1116-23.
An examination of potential matrices for the affinity chromatography of NADP+-linked dehydrogenases with special reference to 6-phosphogluconate dehydrogenase. Biochem J. (1977) 161: 561-8.
Purification and properties of 6-phosphogluconate dehydrogenase from rabbit mammary gland. Biochem J. (1975) 151: 263-70.