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A survey on cytosolic non-enzymic proteins involved in the metabolism of lipophilic compounds: from organic anion binders to new protein families

Bernier, I. ; Jolles, P.

Amsterdam : Elsevier

Biochimie 69 (1987), S. 1127-1152

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ISSN: 0300-9084

Keywords: binding ; comparaison des donnees structurales ; comparison of structural data ; cytosolic non-enzymic proteins ; liasion et transfert de composes lipophiles ; ligand-binding sites ; new intracellular protein families ; nouvelles familles de proteines intracellulaires ; proteines cytosoliques non-enzymatiques ; rapport structure-fonction ; sites de fixation du ligand ; structure-function relationship ; transferring of lipophilic compounds

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0300-9084(87)90140-4

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Amino acid sequence and some ligand binding properties of fatty acid-binding protein from bovine brain (1990)

Schoentgen, F ; Bonanno, L. M. ; Pignède, G. ; [et al.]

Springer

Molecular and cellular biochemistry 98 (1990), S. 35-39

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ISSN: 1573-4919

Keywords: amino acid sequence ; bovine ; brain ; binding

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: 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 µM, Bmax (mol/mol) = 0.6 for oleic acid and Kd = 0.8 µM, 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.