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Journal ArticleDOI

Purification and characterization of fatty acid-binding protein from human placenta.

Tanya Das, +2 more
- 01 Jun 1988 - 
- Vol. 23, Iss: 6, pp 528-533
TLDR
Ouchterlony double immunodiffusion studies have confirmed the immunochemical identity of these three fractions of placental FABP, which revealed that DE-II binds long chain saturated and unsaturated fatty acids nonspecifically, whereas DE-III is mainly an arachidonic acid carrier.
Abstract
Purification of a cytosolic fatty acid-binding protein (FABP) from developing human placenta has been achieved, and its role in modulating the inhibition of human placental glucose-6-phosphate dehydrogenase (G6PD) by palmitoyl-CoA (PAL-CoA) has been studied. FABP was resolved into three peaks, viz. DE-I, DE-II and DE-III, by DEAE cellulose chromatography. DE-I was almost lipid-free. Presence of endogenous fatty acids in DE-II and DE-III was detected by thin layer chromatography (TLC). Fatty acids were the only detectable lipid component in these fractions. Gas liquid chromatography (GLC) analysis revealed that DE-II binds long chain saturated and unsaturated fatty acids nonspecifically, whereas DE-III is mainly an arachidonic acid carrier. Each of these fractions, viz. DE-I, DE-II and DE-III, has a molecular weight of 14,200 Daltons. Ouchterlony double immunodiffusion studies have confirmed the immunochemical identity of these three fractions of placental FABP. Separation in ion exchanger may be due to their different isoelectric points and varied types of binding affinities. Human placental G6PD was inhibited 50% by 0.03 mM PAL-CoA. The DE-II fraction of FABP enhanced the activity of G6PD in the absence of added PAL-CoA and protected against PAL-CoA inhibition of the enzyme. Such a modulating effect of FABP in this inhibition is attributable to binding of long chain acyl-CoA rather than to a direct effect of FABP on the enzyme itself.

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Citations
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Journal ArticleDOI

Characterization of cardiac fatty-acid-binding protein from human placenta. Comparison with placenta hepatic types.

TL;DR: Cardiac FABP acted in a more efficient way as a donor, indicating a distinct role of these proteins in human placenta, which furnishes a multiorgan system for the developing fetus.
Journal ArticleDOI

Inhibition and regulation of rat liver L-threonine dehydrogenase by different fatty acids and their derivatives.

TL;DR: Rat liver L-threonine dehydrogenase is inhibited by several fatty acids and their derivatives: short chain fatty acids, L-2-hydroxybutyrate and D-3-hydroxymalonic acids, such as lauric acid, myristic Acid, palmitic and stearic acids, bicarboxylic acids such as malonic acid and its derivatives methyl- and hydroxymAlonic acids.
Journal ArticleDOI

Human fetal liver fatty acid binding proteins. Role on glucose-6-phosphate dehydrogenase activity.

TL;DR: 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.
Journal ArticleDOI

Macrophages transfer [14C]-labelled fatty acids to pancreatic islets in culture.

TL;DR: It is postulate that in addition to the serum, circulating monocytes may also be a source of fatty acids to pancreatic islets, mainly arachidonic acid.
Journal ArticleDOI

Purification and Characterization of Fatty Acid-Binding Proteins from Human Fetal Lung

TL;DR: Defatted lung FABP reverses the inhibitory effect of palmitoyl coenzyme A (CoA) (PAL- CoA) on lung glucose-6-phosphate dehydrogenase (G6PD), a key enzyme of the hexose monophosphate (HMP) shunt pathway in vitro.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

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Journal ArticleDOI

A simple method for the isolation and purification of total lipides from animal tissues.

TL;DR: In this paper, the authors described a simplified version of the method and reported the results of a study of its application to different tissues, including the efficiency of the washing procedure in terms of the removal from tissue lipides of some non-lipide substances of special biochemical interest.
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Book ChapterDOI

Glucose-6-phosphate Dehydrogenase

TL;DR: G6P-DH is inhibited by primaquine and other 8-aminoquinolines (antimalarial drugs) in millimolar concentration, as well as by phenylhydrazine, Nevertheless, the therapeutic concentration of these substances is more than tenfold lower and therefore, they have no significant effect on the measurements.
Journal ArticleDOI

A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues.

TL;DR: A protein of molecular weight ∼ 12,000 which binds long-chain fatty acids and certain other lipids has been identified in cytosol of intestinal mucosa, liver, myocardium, adipose tissue, and kidney and appears to be identical with the smaller of two previously described cytoplasmic anion-binding proteins.
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