Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels.

A group of low molecular weight fatty acid-binding cytosolic proteins, FABPc, with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABPc with Mr 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABPc from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABPc from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.