Amino acid sequence and some ligand binding properties of fatty acid-binding protein from bovine brain

A fatty acid-binding protein (FABP) from the cytosol of bovine brain was purified by Sephadex G-75 filtration and electrofocusing. The purified protein migrated as a single protein band in 15% polyacrylamide gel electrophoresis with an apparent molecular mass of 14.7 kDa. To ascertain that the purif...

Full description

Saved in:
Bibliographic Details
Published in:Molecular and cellular biochemistry 1990-01, Vol.98 (1-2), p.35-39
Main Authors: Schoentgen, F, Bonanno, L M, Pignède, G, Jollès, P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Brain Chemistry
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cattle
Cytosol - chemistry
fatty acid-binding protein
Fatty Acid-Binding Proteins
fatty acids
Fatty Acids - metabolism
Ligands
Molecular Sequence Data
Myocardium - metabolism
Neoplasm Proteins
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A fatty acid-binding protein (FABP) from the cytosol of bovine brain was purified by Sephadex G-75 filtration and electrofocusing. The purified protein migrated as a single protein band in 15% polyacrylamide gel electrophoresis with an apparent molecular mass of 14.7 kDa. To ascertain that the purified protein was a FABP, it was submitted to fatty acid-binding tests. Oleic and palmitic acids bound to brain FABP but this was not the case for palmitoyl CoA. By Scatchard analysis the ligand binding values were: Kd = 0.28 microM, Bmax (mol/mol) = 0.6 for oleic acid and Kd = 0.8 microM, Bmax (mol/mol) = 2.1 for palmitic acid. The complete amino acid sequence of the brain FABP was determined and a microheterogeneity was observed. Sequence comparison with other FABPs of known sequence and the observed microheterogeneity demonstrated the presence in brain of several homologous FABPs closely related to heart FABP.
ISSN:0300-8177
1573-4919
DOI:10.1007/bf00231365