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Reorganization of Low-Molecular-Weight Fraction of Plasma Proteins in the Annual Cycle of Cyprinidae

A. M. Andreeva1*, N. E. Lamas2,3, M. V. Serebryakova4, I. P. Ryabtseva1, and V. V. Bolshakov1

1Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, 152742 Borok, Russia; fax: (485) 472-4042; E-mail: aam@ibiw.yaroslavl.ru; molbiol@ibiw.yaroslavl.ru; victorb@ibiw.yaroslavl.ru

2Zhirmunsky Institute of Marine Biology, Far-Eastern Branch of the Russian Academy of Sciences, ul. Palchevskogo 17, 690041 Vladivostok, Russia; E-mail: ninalamash@yandex.ru

3Far-Earstern Federal University, ul. Sukhanova 8, 690922 Vladivostok, Russia

4Lomonosov Moscow State University, Leninsky Gory 1, 119991 Moscow, Russia; E-mail: mserebr@mail.ru

* To whom correspondence should be addressed.

Received August 21, 2014; Revision received September 26, 2014
Reorganization of the low-molecular-weight fraction of cyprinid plasma was analyzed using various electrophoretic techniques (disc electrophoresis, electrophoresis in polyacrylamide concentration gradient, in polyacrylamide with urea, and in SDS-polyacrylamide). The study revealed coordinated changes in the low-molecular-weight protein fractions with seasonal dynamics and related reproductive rhythms of fishes. We used cultured species of the Cyprinidae family with sequenced genomes for the detection of these interrelations in fresh-water and anadromous cyprinid species. The common features of organization of fish low-molecular-weight plasma protein fractions made it possible to make reliable identification of their proteins. MALDI mass-spectrometry analysis revealed the presence of the same proteins (hemopexin, apolipoproteins, and serpins) in the low-molecular-weight plasma fraction in wild species and cultured species with sequenced genomes (carp, zebrafish). It is found that the proteins of the first two classes are organized as complexes made of protein oligomers. Stoichiometry of these complexes changes in concordance with the seasonal and reproductive rhythms.
KEY WORDS: fish, plasma proteins, mass spectra, MALDI

DOI: 10.1134/S0006297915020078