Initial studies of the cytoplasmic FABP superfamily.
Our colleagues and we have determined the complete primary structure of a low molecular weight cytoplasmic FABP (also known as z-protein) that binds to LCFAs with high affinities, obtained from rat liver. At the same time, we were the first to propose that rat FABP1, bovine FABP8 (MP-2), bovine CRBP and rat CRABP constituted a protein superfamily in 1982. Since then, extensive investigation of structures, functions and expressions has been carried out on a whole family of FABPs. Analyses of rat heart FABP; FABP1, FABP3 and alpha(2U)-globulin expressed in rat kidney; discovery of ileal FABP6 (I-15P); and first application of FABP2 as a diagnostic marker also stand out in particular.
Department of Biochemistry, School of Medicine, Niigata University, Niigata, Japan. onoteruo@cello.ocn.ne.jp
Teruo
T
Ono
Shoji
S
Odani
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003593:Cytoplasm / Q000378:metabolism*; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D010802:Phylogeny; D051381:Rats
D050556:Fatty Acid-Binding Proteins