Abstract
Aminopeptidase activity was detected in dry and germinating seeds of x Haynaldoticum sardoum. The enzyme was partly purified from germinating seeds and preliminary characterization was carried out. The aminopeptidase showed a pH optimum of 8.0, a molecular weight estimated at 89 000 by Sephadex G-100 gel filtration and an isoelectric point of 4.5. The enzyme hydrolysed p-nitroanilides, but was unable to break down exogenous native proteins. Activity was severely inhibited by p-chloromercuribenzoate, p-hydroxy-mercuribenzoate and bestatin, slightly inhibited by iodoacetamide and ethylenediaminetetraacetic acid and not influenced by 2-mercaptoethanol, phenylmethanesulphonyl fluoride and polyamines. A possible physiological role for the enzyme in the final stages of storage protein degradation is suggested.
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