Open AccessCharacterization of cardiac fatty‐acid‐binding protein from human placenta
Author(s) -
DAS Tanya,
SA Gaurisankar,
MUKHERJEA Manju
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb17602.x
Subject(s) - fatty acid binding protein , sephadex , human placenta , molecular mass , size exclusion chromatography , placenta , chemistry , biochemistry , fatty acid , amino acid , chromatography , fetus , biology , enzyme , pregnancy , genetics , gene
When a 105 000Xg supernatant of human placenta was incubated with [1‐ 14 C]oleate and subjected to Sephadex G‐75 gel filtration and HPLC, two fatty‐acid‐binding protein (FABP) peaks were obtained. One of these, when further purified by carboxymethyl‐cellulose, gave one 15.3‐kDa FABP with p I 5.3. The other, when chromatographed on DEAE cellulose, separated into two 14.2‐kDa FABP with p I 6.9 and 5.4. Purity of the proteins was checked by SDS/PAGE. Molecular mass, p I , immunochemical properties and amino acid compositions all indicated that 15.3‐kDa FABP was of the cardiac type, whereas both 14.2‐kDa FABP were of the hepatic type. Cardiac FABP did not cross‐react with hepatic proteins. When tested for the acceptor/donor properties of these FABP, hepatic types were found to be better candidates than cardiac in uptaking fatty acids from liposomes. Cardiac FABP, on the other hand acted in a more efficient way as a donor, indicating a distinct role of these proteins in human placenta, which furnishes a multiorgan system for the developing fetus.