Isolation and properties of a fatty acid-binding protein from the Pacific lamprey (Lampetra tridentata).
1. A survey of 12 vertebrate species showed that palmitate was bound by an albumin-like serum protein in all classes tested except the dogfish and the lamprey. 2. The major palmitate-binding protein of the Pacific lamprey was isolated and found to be of molecular mass 19,000. 3. The amino acid composition of this protein indicates that it is not a member of the albumin superfamily. 4. The 19-kDa lamprey protein binds bilirubin, cortisol and tryptophan only weakly, but binds palmitate with KA = 25 microM-1, comparable to the first long-chain fatty acid site of bovine albumin (KA = 34 microM-1).
Peters
T
T
Medical Research Institute, Mary Imogene Bassett Hospital, Cooperstown, NY 13326.
Davidson
L K
LK
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000097:blood* / Q000737:chemistry / Q000276:immunology; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D006801:Humans; D007120:Immunochemistry; D007700:Kinetics; D007798:Lampreys / Q000097:blood*; D008970:Molecular Weight; D009363:Neoplasm Proteins; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000097:blood; D013045:Species Specificity; D025521:Tumor Suppressor Proteins; D014714:Vertebrates / Q000097:blood
D000596:Amino Acids; D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D010169:Palmitic Acids; D025521:Tumor Suppressor Proteins; D019308:Palmitic Acid