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Properties and immobilization of urease from leaves of Chenopodium album (C3)



Properties and immobilization of urease from leaves of Chenopodium album (C3)



Botanical Bulletin of Academia Sinica 42(4): 251-258



In C. album, leaf excision and light both increase urease (EC. 3.5.1.5) activity. Dithiothreitol (DTT), reduced glutathione (GSH), cysteine and diazoinedicarboxylic acid bis (N,N-dimethylamide) (diamide) activated the crude enzyme. In contrast, crude urease was inhibited by phenylmethylsulphonyl fluoride (PMSF) and N- alpha -p-tosyl-L-lysine chloromethyl ketone HCl (TLCK), suggesting the presence of serine and histidine residues in the active site.

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