Collection of Czechoslovak Chemical Communications - digital archive 

Abstract

A comparison of eight types of carriers for purification of S-adenosyl-L-homocysteine hydrolase by affinity chromatography is described. The Sepharose-based carriers contained stereoisomeric eritadenines bonded by the carboxyl function or neutral aliphatic adenine derivatives bonded by the amino group of substituent on the heterocyclic nucleus or in the side-chain. Materials with bonded isomeric 9-(RS)-(3(2)-(3-aminopropylamino)-2(3)-hydroxypropyl)-8-hydroxyadenines (VIIIb, IXb) appeared to be carriers of choice which enabled an efficient affinity purification of the enzyme from rat liver. SAH-Hydrolase was liberated only upon elutions with dilute adenosine solutions.