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.
Nielsen
S U
SU
Institute of Medical Biochemistry, University of Aarhus, Denmark.
Pedersen
A O
AO
Vorum
H
H
Brodersen
R
R
D002352:Carrier Proteins / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism; D006801:Humans; D007526:Isoelectric Point; D009206:Myocardium / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry; D009363:Neoplasm Proteins; D011489:Protein Denaturation; D012995:Solubility; D025521:Tumor Suppressor Proteins
D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D009211:Myoglobin; D009363:Neoplasm Proteins; D025521:Tumor Suppressor Proteins