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Piersma, S.R. (author), van de Pijpekamp, A. (author), Wijngaards, G. (author), Gruppen, H. (author), Boumans, H. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
A mass spectrometric approach was chosen to quantify and localise in vitro enzymatically modified glutamine (Gln) residues in a glutamine-rich protein. This protein (named dB1), a cloned domain of the high molecular weight wheat glutenin subunit Dx5, was modified by microbial transglutaminase (TGase) using hydroxylamine as the amine donor. Using...
article 2002