Journal ArticleDOI
Human fetal liver fatty acid binding proteins. Role on glucose-6-phosphate dehydrogenase activity.
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TLDR
F fetal liver FABPs play a regulatory role in critical aspects of cellular physiology during human embryogenesis and protect glucose-6-phosphate dehydrogenase from the feed-back inhibition exerted by added palmitoyl-CoA and oleate.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1989-04-03. It has received 16 citations till now. The article focuses on the topics: Fatty acid synthesis & Fatty acid-binding protein.read more
Citations
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Journal ArticleDOI
Structural and functional features of different types of cytoplasmic fatty acid-binding proteins
TL;DR: Article de synthese sur les donnees recentes de caracteristiques structurales et physicochimiques de divers types of proteines de liaison aux acides gras, avec la signification physiologique de ces diversites.
Journal ArticleDOI
Functions of fatty acid binding proteins.
TL;DR: A considerable body of indirect evidence is provided supporting a broad role for the FABP in the intracellular transport and metabolism of long-chain fatty acids and the existence of structure- and tissue-specific specialization of function among different members of the F ABP gene family.
Journal ArticleDOI
Fatty acid binding protein isoforms: structure and function
TL;DR: Which FABPs form biochemically defined or true isoforms versus FABP that form additional forms, operationally defined as isoforms, is critically evaluated.
Journal ArticleDOI
Acyl-CoA binding proteins: Multiplicity and function
Ruanna E. Gossett,Andrey Frolov,John B. Roths,W. David Behnke,Ann B. Kier,Friedhelm Schroeder +5 more
TL;DR: The identity, nature, function, and pathobiology of these fascinating newly discovered long-chain fatty acyl-CoA binding proteins are explored.
Journal ArticleDOI
Isoforms of rat liver fatty acid binding protein differ in structure and affinity for fatty acids and fatty acyl CoAs.
TL;DR: Rat L-FABP isoforms differ markedly in both structure and ligand binding function, and displacement studies indicated that each isoform displayed distinct specificities for fatty acid/fatty acyl CoA chain length and unsaturation.
References
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Journal ArticleDOI
On the importance of being ionized.
TL;DR: A survey of metabolic reactions discloses that all the known lowmolecular weight and water-soluble biosynthetic intermediates possess groups that are essentially completely ionized at neutral pH, which should have value in guiding investigation of undisclosed biosynthesis reactions.
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A low-molecular-weight protein from rat liver that resembles ligandin in its binding properties.
TL;DR: A protein of S20,W 1.6S and mol.wt.
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A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis.
TL;DR: Bovine liver was shown to contain a hitherto undescribed medium-chain acyl-CoA-binding protein that co-purifies with fatty-acid-binding proteins, but was, unlike these proteins, unable to bind fatty acids.
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Tissue expression of three structurally different fatty acid binding proteins from rat heart muscle, liver, and intestine.
Nathan M. Bass,Joan A. Manning +1 more
TL;DR: Three structurally different 14-15 kDa fatty acid binding proteins have have been purified from rat liver, small intestinal epithelium, and heart muscle, and were quantitated using specific antisera in rat tissues to suggest that they may perform different specific functions in fatty acid transport and metabolism.
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Isolation and characterization of the three fractions (DE‐I, DE‐II and DE‐III) of rat‐liver Z‐protein and the complete primary structure of DE‐II
TL;DR: The complete sequence of Z-protein showed striking homology to cellular retinoid binding proteins and peripheral nerve myelin P2 protein, which indicated the presence of a new family of cellular lipid-binding proteins diverged from a common ancestor.