ArticleFish physiology and biochemistry2016
Structural and biochemical characterization and evolutionary relationships of the fatty acid-binding protein 10 (Fabp10) of hake (Merluccius hubbsi).
Article in Fish physiology and biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 12 citations in OpenAlex.
- Integrated Transcriptomic and Metabolomic Analyses Reveal Physiological and Hepatic Metabolic Responses of Largemouth Bass (International journal of molecular sciences · 2025Article
- Fatty acid binding to the human transport proteins FABP3, FABP4, and FABP5 from a Ligand's perspective.The Journal of biological chemistry · 2024Article
- Molecular Characteristics of the Fatty-Acid-Binding Protein (FABP) Family inAnimals : an open access journal from MDPI · 2023Article
- Tracing the evolution of fatty acid-binding proteins (FABPs) in organisms with a heterogeneous fat distribution.FEBS open bio · 2020Article
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2 authors at 1 institution in 1 country.
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Abstract
A fatty acid-binding protein (FABP) from the liver of Argentine hake (Merluccius hubbsi) was isolated and characterized and its expression analyzed. The determination of its partial primary structures (72%) showed that it presents highest identity with Fabp10, commonly termed liver basic-type FABP. The evolutionary tree showed greater relationship between the Fabp10 of hake (Me Fabp10) and the Fabp10 and the Fabp10a of teleost fish. Me Fabp10 had low affinity for palmitic, oleic and palmitoleic acid and high affinity for bilirubin, lysophosphatidylcholine and lysophosphatidylethanolamine, all of them important in the metabolic functions of the liver. Me Fabp10 was able to bind only one cis-parinaric acid molecule and was found to be expressed only in the liver.
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