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A proteomic approach to verify in vivo expression of a novel γ‐gliadin containing an extra cysteine residue
Author(s) -
Ferrante Paola,
Masci Stefania,
D'Ovidio Renato,
Lafiandra Domenico,
Volpi Chiara,
Mattei Benedetta
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500236
Subject(s) - gliadin , glutenin , gluten , cysteine , chemistry , biochemistry , residue (chemistry) , gene , enzyme , protein subunit
Gliadins and glutenins are the main protein fractions present in wheat gluten. They are responsible for technological and nutritional quality of wheat based products. In particular, glutenins are mainly responsible for dough visco‐elastic properties, whereas gliadins confer extensibility to dough and are the most important factor triggering celiac disease, the major human intolerance to gluten. Gliadins are monomeric proteins, whereas glutenins are polymers stabilized by disulfide bonds. Although they have distinctive structural characteristics, it is possible that some gliadins become part of the glutenin fraction because of mutations that affect cysteine number and distribution. Here, we provide evidence that a naturally mutated γ‐gliadin with an extra cysteine residue is incorporated into the polymeric fraction. This goal was achieved using an integrated approach involving heterologous expression, 2‐DE, RP‐HPLC and MS.