{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,12]],"date-time":"2026-04-12T09:00:01Z","timestamp":1775984401617,"version":"3.50.1"},"reference-count":43,"publisher":"Cambridge University Press (CUP)","issue":"4","license":[{"start":{"date-parts":[[2012,9,25]],"date-time":"2012-09-25T00:00:00Z","timestamp":1348531200000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Seed Sci. Res."],"published-print":{"date-parts":[[2012,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>During the maturation of dicotyledonous seeds, organic carbon, nitrogen and sulphur are stored in protein storage vacuoles (PSVs) as storage globulins. Several studies point to the coexistence of storage proteins with proteases responsible for their degradation inside PSVs. Different mechanisms have been proposed to explain why there is no proteolysis during this period. Protein aggregation to form large supramolecular structures resistant to proteolytic attack could be the reason. However, during germination, and particularly following its completion, the globulin aggregates must undergo disintegration to allow protease attack for protein reserve mobilization. Based on the well-described concentration-dependent ability of Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup> to promote <jats:italic>in vitro<\/jats:italic> aggregation and disaggregation of globulins, we explored a possible role for these alkaline earth cations in globulin packaging and mobilization. Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup> measurements in purified PSVs [6.37\u00a0\u03bcmol and 43.9\u00a0\u03bcmol\u00a0g<jats:sup>\u2212\u00a01<\/jats:sup> dry weight (DW) of cotyledons, respectively] showed the presence of these two alkaline earth cations within this compartment. To our knowledge, this is the first time that Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup> have been quantified in purified PSVs from <jats:italic>Lupinus albus<\/jats:italic> seeds. Considering the importance of these two alkaline earth cations inside PSVs, which represent 14.6% and 60.7% of the total seed Mg<jats:sup>2+<\/jats:sup>and Ca<jats:sup>2+<\/jats:sup>, respectively, globulin aggregation and disaggregation profiles were assayed using experimental conditions closer to those that are physiologically present (proportion of Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup>, and acidic pH). Based on: (1) the high <jats:italic>in vivo<\/jats:italic> abundance of Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup> inside PSVs; and (2) globulin aggregation and disaggregation profiles, together with structural and physiological evidence already reported in the literature, an important physiological role for Ca<jats:sup>2+<\/jats:sup> and Mg<jats:sup>2+<\/jats:sup> in globulin packaging and mobilization inside PSVs is suggested.<\/jats:p>","DOI":"10.1017\/s0960258512000177","type":"journal-article","created":{"date-parts":[[2012,11,9]],"date-time":"2012-11-09T11:11:14Z","timestamp":1352459474000},"page":"249-258","source":"Crossref","is-referenced-by-count":6,"title":["Missing pieces in protein deposition and mobilization inside legume seed storage vacuoles: calcium and magnesium ions"],"prefix":"10.1017","volume":"22","author":[{"given":"Cl\u00e1udia N.","family":"Santos","sequence":"first","affiliation":[]},{"given":"Marta 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