Open AccessAffinity Chromatography on Immobilised Adenosine 5′‐monophosphate
Author(s) -
Harvey Michael J.,
Dean Peter D. G.,
Lowe Christopher R.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03277.x
Subject(s) - elution , chemistry , adsorption , chromatography , ionic strength , affinity chromatography , lactate dehydrogenase , sepharose , activation energy , enzyme , dehydrogenase , arrhenius equation , alcohol dehydrogenase , yeast , biochemistry , organic chemistry , aqueous solution
Icreased temperatures decrease the affinity of glycerokinase and yeast alcohol dehydrogenase for N 6 ‐(6‐aminohexyl)‐5′‐AMP‐Sepharose. Energies of adsorption can be calculated from Arrhenius plots but need to be corrected for the effects of temperature on the ionic strength of the eluant. The energy of adsorption of lactate dehydrogenase using NADH as a specific eluant was shown to have a minimum value of 54.6 kJ/mol (13.0 kcal/mol). Linear gradients of temperature can be successfully employed for the elution of enzymes from affinity adsorbents.