UDP-glucose pyrophosphorylase was purified from germinated barley (malt) using anion exchange and hydrophobic interaction chromatography followed by preparative gel filtration. Gel filtration and SDS-PAGE revealed a molecular mass of 51 to 54 kDa for the monomeric protein. Microsequencing of the blotted protein by Edman degradation gave 20 N-terminal amino acids. UDP-glucose pyrophosphorylase from malt could be markedly stabilized by the addition of bovine serum albumin. The enzyme preparation is free of contaminating nucleoside triphosphatases (UTPases) and can be utilized for the enzymatic synthesis of activated sugars.