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|Title:||Identification of a serine protease inhibitor homologue in Bird's Nest by an integrated proteomics approach||Authors:||Ou, K.
Two-dimensional gel electrophoresis
|Issue Date:||2001||Citation:||Ou, K.,Seow, T.K.,Liang, R.C.M.Y.,Lee, B.W.,Goh, D.L.M.,Chua, K.Y.,Chung, M.C.M. (2001). Identification of a serine protease inhibitor homologue in Bird's Nest by an integrated proteomics approach. Electrophoresis 22 (16) : 3589-3595. ScholarBank@NUS Repository. https://doi.org/10.1002/1522-2683(200109)22:163.0.CO;2-J||Abstract:||For centuries, the edible nests of Collocalia spp. ("Bird's Nests") have been used as a Chinese delicacy that had been claimed to be an effective health-giving tonic. However, clinical studies indicated that in Singapore, Bird's Nest is the most common cause of food-induced anaphylaxis in children, which could lead to potentially life-threatening allergenic reactions. The purpose of this study was to characterize the major allergens in Bird's Nest by using the combined technologies of two-dimensional gel electrophoresis (2-DE), immunochemistry, N-terminal protein sequencing, and mass spectrometry. Results from the immunostaining of the Western blots of the Bird's Nest 2-DE separated proteins with the sera from allergic patients indicated the presence of a major allergen of 66 kDa. Initial searches of the matrix assisted laser desorption/ionization - time of flight - mass spectrometry (MALDI-TOF-MS) tryptic peptide masses of the allergen in the SWISS-PROT and NCBI nonredundant databases revealed that this protein was novel. Based on the partial protein sequence information obtained from N-terminal microsequencing and nanoelectrospray-tandem MS, the 66 kDa immunoreactive allergen was found to be homologous to ovoinhibitor, a Kazal-type serine protease inhibitor, which is one of the dominant allergens found in chicken egg white.||Source Title:||Electrophoresis||URI:||http://scholarbank.nus.edu.sg/handle/10635/111039||ISSN:||01730835||DOI:||10.1002/1522-2683(200109)22:163.0.CO;2-J|
|Appears in Collections:||Staff Publications|
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