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Species difference of liver cytosolic fatty acid‐binding protein in rat, mouse and guinea pig
Author(s) -
Kawashima Yoichi,
Tachibana Yuka,
Nakagawa Sayuri,
Kozuka Hiroshi
Publication year - 1984
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534479
Subject(s) - cytosol , guinea pig , oleic acid , fatty acid binding protein , biochemistry , clinical chemistry , binding protein , biology , fatty acid , microbiology and biotechnology , endocrinology , enzyme , gene
Binding properties of liver cytosolic protein for oleic acid, palmitoyl‐CoA and bromosulphophthalein (BSP) were compared for rat, mouse and guinea pig. Hepatic cytosol of rat, mouse and guinea pig contained proteins with a molecular weight of ca. 12,000 and had an affinity for [1‐ 14 C]‐oleic acid. The concentration of fatty acid‐binding protein (FABP) was almost the same in livers of the animals of the 3 species and was ca. 50 μg/mg cytosolic protein. Electrophoretic studies revealed that FABP from hepatic cytosol of rat, mouse and guinea pig, purified with affinity chromatography, are distinct from one another in terms of their charge. FABP of rat liver was capable of binding any 3 ligands‐oleic acid, palmitoyl‐CoA and BSP—at relatively high binding capacity. FABP of mouse liver also bound oleic acid and palmitoyl‐CoA to a great extent, but its binding capacity for BSP was only one‐third that of rat liver. FABP of guinea pig liver bound less oleic acid and palmitoyl‐CoA than rat liver, whereas it had almost the same binding capacity for BSP as rat liver.