Purification and characterization of fatty acid binding protein in mammalian lung.
A fatty acid-binding protein (FABP) has been isolated and characterized from rat lung tissue. Rat lung FABP has a slightly higher molecular weight than liver FABP, but immunologically, lung FABP is similar to that of liver FABP. Long chain acyl CoA synthetase, a key enzyme in fatty acid metabolism is stimulated by partially purified lung FABP, suggesting a physiologic role of the protein in the activation of long chain fatty acids in pulmonary tissue.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003066:Coenzyme A Ligases / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005779:Immunodiffusion; D008099:Liver / Q000032:analysis; D008168:Lung / Q000032:analysis*; D008297:Male; D008970:Molecular Weight; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D002352:Carrier Proteins; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D009829:Oleic Acids; D010169:Palmitic Acids; D019301:Oleic Acid; D019308:Palmitic Acid; D003066:Coenzyme A Ligases