Structural and biochemical characterization and evolutionary relationships of the fatty acid-binding protein 10 (Fabp10) of hake (Merluccius hubbsi)

被引：8
|
作者：
Alejandra Crovetto, Cecilia [1 ]
Leon Cordoba, Osvaldo [1 ]
机构：
[1] Univ Nacl Patagonia San Juan Bosco, Fac Ciencias Nat, GQBMRNP CRIDECIT, Dept Bioquim, 9000 Comodoro Rivadavia, Chubut, Argentina
来源：
FISH PHYSIOLOGY AND BIOCHEMISTRY | 2016年 / 42卷 / 01期
关键词：
Hake; Fatty acid-binding protein; Liver; Fabp10; TISSUE-SPECIFIC EXPRESSION; SEQUENCE DETERMINATION; CRYSTAL-STRUCTURE; MULTIGENE FAMILY; LIVER; GENES; HEART; PURIFICATION; TRANSPORT; ADIPOCYTE;
D O I：
10.1007/s10695-015-0126-x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：149 / 165
页数：17
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