Abstract
A search and identification of osmotically active proteins (OAP) in the composition of blood serum anodic fraction from Atlantic cod Gadus morhua were undertaken using polyacrylamide gel electrophoresis and MALDI mass-spectrometry. 17 OAP have been identified. According to the annotations of Gene Ontology for candidates, 13 OAP were classified as extracellular and 4 OAP- as intracellular proteins. The relative content of OAP in cod serum was ~50% of the total protein. Extracellular proteins apolipoproteins (in the composition of high-density lipoproteins) and hemopexin were dominated in OAP pool. Moreover, the relative content of ApoA-I was ~25% of the total serum protein. Of the intracellular proteins on the serum proteomic map, low molecular weight fragments of the myosin heavy chain were dominated. The results obtained are consistent with the provisions of the “albumin-free” hypothesis of capillary exchange, which considers multiple extracellular and intracellular proteins from different functional classes as osmotically active plasma proteins of “albumin-free” teleost fish.
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