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Vol 47(2013) N 6 p. 885-893; I.A. Popov1,2,3,4,5, N.L. Starodubtseva1,2, M.I. Indeikina1,3,5, A.S. Kononikhin1,2,5, M.I. Nikolaeva1, E.N. Kukaev2,5, S.A. Kozin3,4, A.A. Makarov3, E.N. Nikolaev1,2,4,5* Mass Spectrometric Identification of Posttranslational Modifications in Transthyretin from Human Blood 1Talrose Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia2Moscow Institute of Physics and Technology (State University), Dolgoprudny, 141700 Russia 3Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia 4Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, 119121 Russia 5Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119991 Russia *nikolaev@chph.ras.ru Received - 2013-04-15; Accepted - 2013-06-14 Transthyretin, one of the major blood proteins, displays a variety of posttranslational modifications, including those related to the development of grave diseases, such as Alzheimer's disease, and familial amyloid polyneuropathy. A combined analytical technique based on the use of two mass spectrometric approaches (bot-tom-up and top-down) has been developed in the present study to determine the role of the modified forms of transthyretin in the progression of Alzheimer's disease. The high efficiency of this technique has been demonstrated for ten serum samples obtained from patients diagnosed with Alzheimer's disease and healthy volunteers. proteomics, transthyretin, posttranslational modifications, tandem mass spectrometry |
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