Purification and properties of urease from a cyanobacterium Anabaena doliolum

Abstract

Urease was purified 39 fold from extracts of Anabaena doliolum. The enzyme had a MW of 228 000 as determined by gel filtration and consisted of six subunits of identical size with a MW of 36 000. The enzyme activity was optimum at pH 7.0 and at 40°C with a Km of 115 μM. Among the metal ions tested, Hg2+, Ag2+ and Cu2+ inhibited enzyme activity in decreasing order. p-hydroxymercuribenzoate (10 μM) and acetohydroxyamic acid (100 μM) brought about a total inhibition of urease activity. © 1989.