Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor
Identifieur interne : 000281 ( France/Analysis ); précédent : 000280; suivant : 000282Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor
Auteurs : P. Goupil [France] ; Y. Croisille [France] ; F. Croisille [France] ; G. Ledoigt [France]Source :
- Plant Science [ 0168-9452 ] ; 1988.
Abstract
Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from Helianthus tuberosus shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.
Url:
DOI: 10.1016/0168-9452(88)90054-4
Affiliations:
- France
- Auvergne (région administrative), Auvergne-Rhône-Alpes
- Clermont-Ferrand
- Université Blaise-Pascal
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ISTEX:4DCC6B1D18791F89D255959492976DB9B58FB89BLe document en format XML
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