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RESEARCH PRODUCT
Affinity chromatography with triazine dyes immobilized onto activated non-porous monodisperse silicas
Jeffrey R. DaviesMilton T.w. HearnB. AnspachK.k. Ungersubject
ChromatographyElutionOrganic ChemistrySubstrate (chemistry)General MedicineBiochemistryMalate dehydrogenaseAnalytical Chemistrychemistry.chemical_compoundAffinity chromatographychemistryLactate dehydrogenaseSelectivityAldehyde ReductaseTriazinedescription
Abstract Non-porous monodisperse silicas with a particle diameter of 2.1 μm were modified with different silanes for immobilization of various triazine dyes including Procion Red HE3B, Procion Red MX5B, and Cibacron Blue F3GA. Lactate dehydrogenase and malate dehydrogenase from different species and aldehyde reductase from rat brain were purified by affinity elution using the substrate of the enzyme and NADH. With Cibacron F3GA the selectivity for NADH-dependent enzymes was higher than with the two Procion dyes. The utility of these immobilized triazine dye systems on non-porous silica supports for the rapid separation of Cohn Fraction III plasma proteins, including plasminogen, is also described.
year | journal | country | edition | language |
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1988-01-01 | Journal of Chromatography A |