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Characterization of a novel cysteine peptidase from tissue culture of garlic (Allium sativum L.)
Authors:Mónica?Parisi,Silvia?Moreno,Craciela?Fernández  author-information"  >  author-information__contact u-icon-before"  >  mailto:ferngra@mail.unlu.edu.ar"   title="  ferngra@mail.unlu.edu.ar"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Laboratorio de Química Biológica, Departmento de Ciencias Básicas, Universidad Nacional de Luján, CC: 221, Luján (6700), Buenos Aires, Argentina;(2) Instituto de Investigaciones Bioquímicas ‘Fundación Campomar’, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, I.I.B.B.A.-CONICET, Argentina
Abstract:Summary A simple and efficient medium for callus tissue culture from garlic to obtain maximal proteolytic activity is described. Murashige and Skoog basal medium supplemented with 4.44 μM naphthaleneacetic acid (NAA) and 0.54 μM benzyladenine (BA) resulted in the best biomass production and protease expression. The protease activity belongs to the class of cysteine proteases since they are inhibited by E64 and Leupeptin and also they are activated by 2-mercaptoethanol and cysteine. They showed good thermal stability. Three active protease bands were found in zymograms of Allium sativum. The in vitro system revealed a significantly higher protease level than storage and embryo tissues of in vivo bulbs.
Keywords:callus culture  cysteine protease  endopeptidase   in vitro culture  protease modulators
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