BIOLOGIYA MORYA, 2015, Vol. 41, No. 1, pp. 55-63

Structural features of the low-molecular-weight plasma fraction in Far Eastern redfins of the genus Tribolodon and other cyprinid fishes

© 2015 A. M. Andreeva¹, M. V. Serebryakova², N. E. Lamash^3,4, R. A. Fedorov¹, I. P. Ryabtseva¹

¹I.D. Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, Borok 152742;
²Lomonosov Moscow State University, Moscow 119991;
³A.V. Zhirmunsky Institute of Marine Biology, Far East Branch, Russian Academy of Sciences, Vladivostok 690041;
⁴Far Eastern Federal University, Vladivostok 690950

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The organization of the low-molecular fraction (LMF) of proteins from fish plasma is studied in Far Eastern redfins of the genus Tribolodon and other representatives of the family Cyprinidae. The common principle of organization of plasma LMF is established. According to this principle, the LMF includes two subfractions: oligomeric and monomeric proteins. During the pre-spawning period, a decrease in the apparent molecular weight of proteins as a result of changes in their oligomeric structure is observed in the former subfraction; a reduction of heterogeneity of proteins, in the latter subfraction. The analysis of these rearrangements allows differentiating two main types of the LMF: "basic" and "plastic". The former type is characterized by a low level of metabolic processes; the latter one, by their activation during the pre-spawning period. By using MALDI mass spectrometry, polymeric forms of apolipoproteins, fetuin, and albumin-like protein were identified within the oligomeric subfraction; hemopexin and inhibitors of proteinases, within the monomeric subfraction.

Key words: low-molecular proteins of blood plasma, Cyprinidae, 2D-electrophoresis, MALDI mass spectrometry.