Collect. Czech. Chem. Commun. 1983, 48, 2549-2557

Affinity chromatography of rat liver S-adenosyl-L-homocysteine hydrolase

Ivan Votruba, Antonín Holý and Ivan Rosenberg

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6


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.