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Abstract <p>The search and identification of blood serum proteins withhigh osmotic activity (osmotically active proteins, OAP) were carriedout in albumin-containing fish, northern <i>Esoxlucius</i> L., using electrophoresis and MALDI mass spectrometry.Several proteins with high negative charge (8&#xa0;extracellular and1 intracellular) were found and identified in the pike blood serum.The total relative content (TRC) of all OAP was ~60%. The relativecontent (RC) of individual OAP—hemopexin, proteinase inhibitors, apopoproteinA-I (in high density lipoproteins) and albumin—were ~30, ~10, ~12,and 3.6%, respectively; intracellular protein Grb14 was represented bytrace amounts. According to the annotations of Gene Ontology, themain functions of OAP are related to the protection and transport.At the same time, the high negative charge of OAP suggests their highosmotic activity. The comparison of OAP lists in albumin-containingpike and albumin-free fishes shows that they are consistent acrossall extracellular OAP except for albumin, which is negligible inthe pike serum. In light of the albumin-free model of capillaryexchange, these facts do not point to a key role of albumin in osmotichomeostasis control in fish. The multiplicity of OAP in the bloodof teleost fishes distinguishes them from mammals, where serum albuminis a key factor controlling capillary fluid exchange.</p>

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Identification and Characterization of Blood Serum Proteins with High Osmotic Activity in the Pike Esox lucius

  • 期刊论文

  • 发表日期：

    2026年2月26日

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  • A. M. Andreeva,
  • Z. M. Bazarova,
  • M. A. Konstantinov,
  • I. Yu. Toropygin,
  • R. A. Fedorov,
  • D. V. Garina,
  • A. S. Vasiliev

摘要

Abstract

The search and identification of blood serum proteins withhigh osmotic activity (osmotically active proteins, OAP) were carriedout in albumin-containing fish, northern Esoxlucius L., using electrophoresis and MALDI mass spectrometry.Several proteins with high negative charge (8 extracellular and1 intracellular) were found and identified in the pike blood serum.The total relative content (TRC) of all OAP was ~60%. The relativecontent (RC) of individual OAP—hemopexin, proteinase inhibitors, apopoproteinA-I (in high density lipoproteins) and albumin—were ~30, ~10, ~12,and 3.6%, respectively; intracellular protein Grb14 was represented bytrace amounts. According to the annotations of Gene Ontology, themain functions of OAP are related to the protection and transport.At the same time, the high negative charge of OAP suggests their highosmotic activity. The comparison of OAP lists in albumin-containingpike and albumin-free fishes shows that they are consistent acrossall extracellular OAP except for albumin, which is negligible inthe pike serum. In light of the albumin-free model of capillaryexchange, these facts do not point to a key role of albumin in osmotichomeostasis control in fish. The multiplicity of OAP in the bloodof teleost fishes distinguishes them from mammals, where serum albuminis a key factor controlling capillary fluid exchange.