PubMed Health⌕ Search

Biomedical subjects

V Baccari

Publications and source records attributed to V Baccari.

15 recordsLinked to original sources
PubMed1986

Activities of NAD-and NADP-specific isocitrate dehydrogenases in kidney mitochondria of rachitic rat.

In the previous research we have demonstrated that rats fed on a rickets-inducing diet show increasing citrate levels in kidney and intestinal mucosa. The study of the enzymes related to citrate metabolism has shown that both NAD+-and NADP+-dependent isocitrate dehydrogenases decrease in kidney mitochondria of rachitic rat. The inhibitory effect of Ca2+ and citrate on the activity of the two dehydrogenases has been also investigated; these metabolites behave as competitive inhibitors against Mg2+ both in normal and in rachitic rats.

Alkaline Phosphatase↗
PubMed1984

On the interaction between synthetic detergents and enzymatic proteins.

Eight highly purified and crystalline enzymes representative of fundamental metabolic pathways and of cellular structure were tested with seven detergents. The enzyme-detergent interaction was studied as a time-independent (inhibition) or time-dependent (inactivation) phenomenon. Our results imply a specificity of detergent action on the enzymes studied.

Alanine Transaminase↗
PubMed1984

[Interaction : detergents-enzymes].

The study on the action of eight synthetic detergents of various types of well defined structure and properties (neutral, anionic, cationic) has been realized on fourteen highly purified enzymes of animal or vegetal origin of great metabolic importance, on these of homogenates of intestine or liver of normal rats and of rats fed during a relatively long period with food containing synthetic detergents. The action of all studied detergents on highly purified enzymes has been characterized as this of specific effectors, producing a reversible denaturation of enzymatic proteins to whom they combine. Ingestion of detergents by rats leads, probably by the same mechanism, to a diminution in vivo of the activity of some intestinal and hepatic enzymes.

Animals↗
PubMed1983

The palmitoleate: a natural selective denaturant of enzymes.

A study has been carried out in order to explain the enzyme-palmitoleate interaction. The highly purified and crystalline enzymes representative of fundamental metabolic pathways were: alcohol dehydrogenase (ADH), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), isocitrate dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G6P-DH), alkaline phosphatase. The enzyme-palmitoleate interaction was studied as a phenomenon time-independent (inhibition) and time-dependent (inactivation). Palmitoleate inhibited remarkably LDH, MDH, ICDH and G6P-DH. A kinetic analysis of the inhibitory action of palmitoleate on LDH and MDH was also carried out. Inactivation studies have shown that ADH and alkaline phosphatase are not sensitive to palmitoleate action, unlike the other enzymes. A comparison was made between the action of palmitoleate and that of a synthetic anionic detergent, sodium dodecyl sulfate (SDS).

Alcohol Dehydrogenase↗
PubMed1977

Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine.

Recently it has been demonstrated that hydroxylamine is an activator of triglyceride catabolism. We have studied the effect of hydroxylamine on isocitrate lyase activity and lipid catabolism and have noted a stimulation of isocitrate lyase biosynthesis by 5 mM hydroxylamine. The specificity of this effect was tested with a number of representative enzymes of other metabolic pathways. In an attempt to study the possible mechanism of action of hydroxylamine we have also tested the effects of two substances that are structural or functional analogues of hydroxylamine, namely, ethanolamine and hydrazine, both on the enzyme level in plant cultures and on the activity of enzyme preparations. From our data we may conclude that "de nove" biosynthesis of isocitrate lyase depends on the reaction of hydroxylamine or hydrazine with glyoxylate to give the corresponding oxime and hydrazone. The removal of glyoxylate from the biological equilibrium in this way could cause extra formation of isocitrate lyase.

Dose-Response Relationship, Drug↗
PubMed1968

Changes in Enzyme Levels During Germination of Seeds of Triticum durum.

The changes in level of activity during the germination of wheat seedling (Triticum durum) in the dark have been investigated with 4 enzymes of glycolysis, 2 enzymes of the pentose phosphate shunt, 2 of the tricarboxylic acid cycle, 2 of amino acid metabolism and acid phosphatase. For some enzymes, which function in photosynthesis (fructose diphosphate aldolase, glyceraldehyde phosphate dehydrogenase NADP dependent), the level of activity was influenced by the presence of light.

Journal Article↗
PubMed1968

Enzymes of glyoxylate in conifers.

The high level of lipids in seeds of some species of conifers suggested that the glyoxylate cycle might have a role in conifer seed metabolism.Six species (Pinus pinea, Pinus pinaster, Pinus canariensis, Pinus strobus, Abies alba, and Cupressus sempervirens) were investigated for their lipid content and malate synthase and isocitrate lyase level. The fatty acid composition of the triglyceride fraction was also investigated. The correlation between lipid content of germinating seed with the presence of the cycle was confirmed. The enzymes of the glyoxylate cycle were not detected in Cupressus sempervirens where the lipid content is very low.

Journal Article↗