{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T13:31:18Z","timestamp":1762954278417},"reference-count":24,"publisher":"Wiley","issue":"1-3","license":[{"start":{"date-parts":[[2002,12,12]],"date-time":"2002-12-12T00:00:00Z","timestamp":1039651200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2003,1,16]]},"abstract":"<jats:p>Conglutins are multisubunit, glycosylated, major storage proteins present in <jats:italic>Lupinus<\/jats:italic> seeds that self\u2010aggregate in a calcium\/magnesium\u2010dependent manner. Two of these globulins exhibit lectin activity. The 210 kDa globulin derived from \u03b2\u2010conglutin that accumulates in <jats:italic>Lupinus<\/jats:italic> cotyledons during germination was used as a model protein to establish whether the self\u2010aggregation process is electrostatic in nature or lectin\u2010mediated. This protein binds in a very strong manner to chitin and recognizes a variety of glycoproteins including immunoglobulins G. Several compounds were tested for their inhibitory effect on the cation\u2010dependent self\u2010aggregation process. Sialic acid and phytin were the most effective whereas chitin and mucin were totally ineffective. The inability of the oligosaccharidic side chains of the 210 kDa protein, \u03b2\u2010conglutin and immunoglobulin G to interfere with the aggregation strongly supports the view that Ca\/Mg are electrostatically involved in the in vitro self\u2010aggregation of <jats:italic>Lupinus<\/jats:italic> globulins. The results suggest that calcium and magnesium ions are also electrostatically involved in vivo in the macromolecular aggregation of legume seed storage proteins, ensuring their efficient packing inside the protein storage vacuoles. This mechanism is responsible for the typical insolubility of legume globulins in water.<\/jats:p>","DOI":"10.1016\/s0014-5793(02)03801-2","type":"journal-article","created":{"date-parts":[[2003,1,17]],"date-time":"2003-01-17T17:34:03Z","timestamp":1042824843000},"page":"106-110","source":"Crossref","is-referenced-by-count":16,"title":["Self\u2010aggregation of legume seed storage proteins inside the protein storage vacuoles is electrostatic in nature, rather than lectin\u2010mediated"],"prefix":"10.1002","volume":"534","author":[{"given":"Ricardo B.","family":"Ferreira","sequence":"first","affiliation":[]},{"given":"Regina L.","family":"Freitas","sequence":"additional","affiliation":[]},{"given":"Artur R.","family":"Teixeira","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2002,12,12]]},"reference":[{"key":"e_1_2_5_2_1","first-page":"75","volume":"23","author":"M&#x00FC;ntz K.","year":"1985","journal-title":"Physiol. 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