Abstract
Usi>ic acids are powerful cm]zy>]e inactivators, being demonstrated for DNAase (1). glutamate dehydrogenase (2) and urease (a). This ft>>]ction isacommon cl]aracteristic of phenolics (4), cat>5i1]g aggrega— tio>] sUdes wl]ici> increase >nolecular -weigbt of protcins. iZece>lily, VicENTE et al. (5) lave shown that urea, st>bstrate of t>rease, causes itself an aggregation of protein cooperating \vith tl>e L—usm,ic acid— depending aggregatiom]. Tbe aggregates, commol]ly inactive, show a ino!ect>lar wCi (r~>~ hi than ~ gher 800,000. TI>e imiactive aggregates reverse to active protein when theaggre— gation provoled by L—usnic acid is carried out in the presence of 1-— cysteim> (U). Ti>erefore. we shonld reject dic hypothesis referringto the :iggregation state at tlie only responsible for the enzymatic inactivation since active aggregates of high molecular weight have been fonud. The present paper studies tl,e changes in tl]e quaternary struciure of t>rease produced by L—usnic acid depeud ing on tIc tertiary structure of el]zyme.
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