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Biomedical subjects

B Nasser

Publications and source records attributed to B Nasser.

6 recordsLinked to original sources
PubMed2001

Trans- and cis-octadecenoic acid isomers in the hump and milk lipids from Camelus dromedarius.

The distribution profiles of individual trans- as well as cis-18:1 isomers from the fat prepared from the hump adipose tissue and the milk from Camelus dromedarius (the single-humped Arabian species) are described. Gas-liquid chromatography on two capillary columns with different polarities and lengths were used for this purpose in combination with argentation thin-layer chromatography. A comparison of the profiles established is made with that of true ruminant fats. In the fats from the dromedarius as well as from true ruminants, the trans-18:1 isomers have their ethylenic bonds in all positions between delta4 and delta16. The prominent trans isomer is the 11-18:1 (vaccenic) acid in all species, and the complete distribution profiles are quite similar. Concerning the cis isomers, the prominent isomer is oleic acid, followed by cis-vaccenic acid, as in true ruminant fats. Other cis isomers encompass the delta6-8 and the delta12 to delta15 isomers. Camelidae (suborder Tylopoda) and Bovidae (suborder Ruminantia) have evolved independently since the Eocene, that is for approximately 50 million years. Despite this considerable period, and the profound differences in anatomy, morphology, physiology, ecological and dietary habits between the extant species of these suborders, the rumen microflora has continued to synthesize the same trans- and cis-octadecenoic acid isomers, in comparable proportions, at least as deduced from their composition profiles. We conclude that the trans-18:1 acid profile is not intrinsically species-dependent, but it can be affected by the nature and the proportions of dietary unsaturated fatty acids that themselves depend on the feed, and that may be species-specific.

Adipose Tissue↗
PubMed1993

Labeling of the mitochondrial membrane D-3-hydroxybutyrate dehydrogenase (BDH) with new bifunctional phospholipid analogues.

D-3-Hydroxybutyrate dehydrogenase (BDH), an inner mitochondrial protein, is a well-known phospholipid dependent enzyme. It is a primary dehydrogenase of the oxidative phosphorylation system and is involved in the redox balance of the NAD+/NADH pool. The preparation of fluorescent phospholipids and newly synthesized bifunctional phospholipid analogues (fluorescent and photoactivatable) allowed us to study the structural requirement for lipid activation of the purified enzyme. This paper reports the chemical synthesis protocols to prepare these new phospholipids and their characterization. Illumination experiments of complexes between bifunctional phospholipids and BDH which lead to a cross-linked polypeptide indicate that both the polar head and the hydrophobic moiety of phospholipids interact with BDH. The bifunctional phospholipids were also tested on other lipid-binding proteins, i.e., horse cytochrome c and bovine serum albumin, and demonstrated the promising potential of this new type of photoactivatable molecules which can be followed merely by fluorescence without radioactive labeling.

Enzyme Activation↗
PubMed1991

Interactions of the mitochondrial membrane rat liver D-3-hydroxybutyrate dehydrogenase with glass beads during adsorption chromatography. Relationships with the activation of the enzyme by phospholipids.

D-3-Hydroxybutyrate dehydrogenase (BDH) is an NAD(+)-dependent dehydrogenase of the mitochondrial inner membrane involved in the energetic balance between the liver and peripheral organs in mammals. It allows the conversion of ketone bodies (acetoacetate and D-3-hydroxybutyrate) and it is one of the best documented lipid-requiring enzymes with a dependence on lecithins. After release of proteins from the membrane by phospholipase A2 treatment of salt-treated mitochondria, the rat liver enzyme is absorbed on controlled-pore glass beads. After batch washing, the enzyme, devoid of lipids (apoBDH), is specifically eluted at pH 8.05-8.15 with a 0.1 M Tris-1 M LiBr buffer under reducing conditions (5 mM dithiothreitol). It appears that during BDH absorption, the glass beads mimic the phospholipid surface of biomembranes.

Animals↗
PubMed1988

[Effects of synthetic bioactive lipids on the activity of D-beta-hydroxybutyrate dehydrogenase, a membrane enzyme].

The structural requirements of lecithins analogs for purified D-beta-hydroxybutyrate dehydrogenase activation have been studied with chemically defined phospholipids. It appears that the trimethylamine group of choline can be changed by a pyridinium group. On the other hand, the decrease of density of the positive charges on the liposomes surface obtained by dilution of such bearing molecules with negative or non charged phospholipids increases the enzyme reactivation. Finally, the PAF acether, a lipid mediator, is able to reactivate the enzyme in similar conditions as these obtained with mitochondrial phosphatidylcholines.

Chemical Phenomena↗
PubMedDate not supplied

Phospholipid polar head specificity of D-3-hydroxybutyrate dehydrogenase activation studied by new synthetic phospholipids and analogues.

D-3-hydroxybutyrate dehydrogenase, an inner-mitochondrial enzyme responsible for the interconversion of two ketone bodies, is a well known phospholipid dependent enzyme. Newly synthesized phospholipid analogues were used to study the structural requirement for lipid activation of the purified enzyme. A positive charge on the polar head is required but must be at the surface of lipid vesicles. In contrast the maximum velocity and the Michaelis constant values are not strongly dependent on the nature of the zwitterionic phospholipid polar head.

Animals↗