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| Content Provider | Springer Nature Link |
|---|---|
| Author | Crovetto, Cecilia Alejandra Córdoba, Osvaldo León |
| Copyright Year | 2015 |
| 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. |
| Starting Page | 149 |
| Ending Page | 165 |
| Page Count | 17 |
| File Format | |
| ISSN | 09201742 |
| Journal | Fish Physiology and Biochemistry |
| Volume Number | 42 |
| Issue Number | 1 |
| e-ISSN | 15735168 |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2015-09-14 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Hake Fatty acid-binding protein Liver Fabp10 Freshwater & Marine Ecology Animal Physiology Animal Anatomy / Morphology / Histology Animal Biochemistry Zoology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Medicine Biochemistry Aquatic Science |
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