Lupin conglutins

Dooper MMBW, Plassen C, Holden L, Lindvik H, F ste CK (2009). IgE cross-reactivity between lupin conglutins and peanut allergens in serum of lupin-allergic individuals. J. Investig. Allergol. Clin. Immunol, 19 283-291. 

Furthermore, a novel polyclonal/monoclonal-based sandwich ELISA for the detection of lupin proteins in foods was described (Holden et al., 2007). The monoclonal antibody reacts specifically with a-conglutin (Dooper et al., 2007). The assay has a detection limit of Img protein/kg food and is sensitive to both native and processed proteins from L. angustifolius and L. albus. A selection of 112 food samples, both with and without lupin declaration, was analyzed showing that the majority of products were labeled correctly. 

DurantiM, Gius C, Sessa F, Vecchio G (1995). The saccharide chain of lupin seed conglutin gamma is not responsible for the protection of the native protein from degradation hy trypsin, hut facilitates the refolding of the acid-treated protein to the resistant conformation. Eur. J. Biochem., 230 886-891. 

DurantiM, Sessa F, ScarafoniA, Bellini T, DallocchioF (2000). Thermal stabilities of lupin seed conglutin gamma protomers and tetramers. J. Agric. Eood Chem., 48 1118-1123. 

Duranti M, Di Cataldo A, Sessa F, Scarafoni A, Ceciliani F (2002). Metal ions restore the proteolytic resistance of denatured conglutin gamma, a lupin seed glycoprotein, by promoting its refolding. J. Agric. Food. Chem., 50 2029-2033. 

Foss N, Duranti M, Magni C, Frokiaer H (2006). Assessment of lupin allergenicity in the cholera toxin model induction of IgE response depends on the intrinsic properties of the conglutins and matrix effects. Int. Arch. Allergy. Immunol, 141 141-150. 

Magni C, Sessa F, Accardo E, et al. (2004). Conglutin gamma, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J. Nutr. Biochem., 15 646-650. 

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