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Biomedical subjects

I Singh

Publications and source records attributed to I Singh.

At least 307 records · Page 17Linked to original sources
PubMed1983

Degradation of myelin proteins by brain endogenous neutral protease.

A proteolytic enzyme isolated from calf brain cytosol, degraded purified myelin basic protein in the presence of Ca2+ at pH 7.0 (Singh, I. and Singh, A.K., Trans. Amer. Soc. Neurochem., 13 (1982) 119). This proteolytic enzyme also degrades basic proteins when incubated with intact myelin in the presence of Ca2+ at a neutral pH. Three hour treatment of purified myelin with this protease resulted in degradation of large basic protein and small basic protein by 73 and 89%, respectively. This proteolytic activity was inhibited by EDTA, leupeptin and low pH (pH 4.0), but was not affected by phenylmethylsulfonylfluoride, p-nitrophenylguanidinobenzoate and pepstatin A. Purified myelin preparations also contain small amounts of Ca2+-activated proteolytic activity. The fact that this is a neutral protease, endogenous to the brain, suggests that it may play a role in the degradation of myelin under physiological and pathological conditions.

Animals↗
PubMed1983

Ceramide synthesis from free fatty acids in rat brain: function of NADPH and substrate specificity.

At the subcellular level, the synthesis of ceramide from free lignoceric acid and sphingosine in brain required reconstituted enzyme system (particulate fraction, heat-stable and heat-labile factors) and pyridine nucleotide (NADPH). The mitochondrial electron transfer inhibitors (KCN and antimycin A), energy uncouplers (oligomycin and 2,4-dinitrophenol), and carboxyatractyloside, which prevents the transport of ATP and ADP through the mitochondrial wall, inhibit the synthesis of ceramide in the presence of NADPH but have very little effect in the presence of ATP. Similar to the synthesis of ceramide, the synthesis of ATP from NADPH and NADH by the particulate fraction also required cytoplasmic factors (heat-stable and heat-labile factors). Moreover, ATP, but not its analog (AMP-CH2-P-O-P), can replace NADPH, thus suggesting that the function of the pyridine nucleotide is to provide ATP for the synthesis of ceramide. The cytoplasmic factors were not required for the synthesis of ceramide in the presence of ATP. The maximum velocity for synthesis of ceramide from free fatty acids of different chain lengths (C16-C26) was bimodal, with maxima around stearic acid (C18) and behenic acid (C22). The relative rate of synthesis of ceramide parallels the relative distribution of these fatty acids in brain cerebrosides and sulfatides.

Animals↗
PubMed1983

Effect of diethylcarbamazine citrate on Angiostrongylus malaysiensis infection in rats.

The aim of the study was to observe the effect of diethylcarbamazine citrate (DEC) on Angiostrongylus malaysiensis infection in albino rats. An attempt was made to vary the dose of DEC and treat infected animals at the larval and adult stages of infection. The doses were varied with an aim at finding an effective dosage. Animals were treated also during the pre-infection period to observe if the drug had any prophylactic properties. The results obtained show that DEC given after infection was effective only when its administration was initiated on day 42 of the infection corresponding to the mature adult stage of the parasite. In addition, it had some prophylactic activity against the infection.

Angiostrongylus↗
PubMed1983

Effect of cyclodextrins on the solubilization of lignoceric acid, ceramide, and cerebroside, and on the enzymatic reactions involving these compounds.

alpha-Cyclodextrin at concentrations of 1-8 mM helps dissolve, in aqueous solution, fatty acids such as lignoceric, stearic, and palmitic, and complex lipids such as ceramide and cerebroside that contain these acids. Formation of an inclusion complex was indicated on examination of the solution by gel filtration. alpha-Cyclodextrin strikingly increased synthesis of ceramide from sphingosine and either free lignoceric or stearic acid by rat brain preparations. These results suggest the further use of alpha-cyclodextrin in lipid enzymology, especially in relation to sphingolipid metabolism.

Animals↗
PubMed1982

Brain-specific ceramide synthesis activity: change during brain maturation and in jimpy mouse brain.

The synthesis of ceramide from lignoceric acid was studied in normally developing rat brain and jimpy mouse brain. The developmental pattern of the synthesis of both non-hydroxy and hydroxyceramide from free lignoceric acid in a brain-specific pathway requiring NADPH and cytosolic factors was similar to the synthesis from lignoceroyl CoA and both showed increasing activity during myelination. There were no differences in non-hydroxyceramide synthesis between jimpy and normal littermate control mouse brains by both pathways. HPLC analysis showed the same non-hydroxyceramide level in both types of brains.

Aging↗
PubMed1982

Mutagenicity of HPLC fractions from extracts of AAtrex-treated corn.

Crude extracts from maize plants treated with varying concentrations of AAtrex, an s-triazine herbicide, were tested for the induction of gene conversion in a diploid strain of Saccharomyces cerevisiae heteroallelic at two loci. These extracts were then subjected to analysis by higher pressure liquid chromatography (HPLC), and the fractions collected in water, 50% methanol, and 100% methanol were similarly tested. Dose-dependent convertogenic activity observed in the 50% methanol fractions suggested that the mutagen(s) is recovered in this fraction.

Atrazine↗
PubMed1981

Effect of alpha-actinin on actin structure. Actin ATPase activity.

Alpha-Actinin increases the ATPase activity of actin by up to 84%, depending un pH, divalent cations present and the added Mg2+: ATP ratio. Dithiothreitol decreases actin ATPase activity approx. 20% but does not reduce the ability of alpha-actinin to increase actin ATP activity. Increasing amounts of added alpha-actinin up to 1 mos alpha-actinin to 49 mol actin cause in increasing increment in actin ATPase activity, but adding alpha-actinin beyond 1 mol alpha-actinin to 49 mol actin elicits only small additional increments in activity. Actin ATPase activity ranges from approx 100 nmol Pi/mg actin per h (4.3 mol Pi/mol actin per h) at high levels (10 mM) of ATP in the presence of lower amounts (1 mM) of added mg2+ to approx. 12.5 nmol Pi/mg actin per h (0.52 mol Pi/mol actin per h) at high pH (8.5) or at low levels (0.5-1.0 mM) of ATP in the presence of higher amounts (10 mM) of added Mg2+ ATp uncomplexed with Mg2+ inhibits the ability of alpha-actinin to increase F-actin ATPase activity. Activities with different divalent cations showed that the actin ATPase in these studies, which was 1/100 as great as Mg2+-modified actomyosin ATPase activity, was not due to trace amounts of myosin contaminating the actin preparations. The results are consistent with the concept that alpha-actinin can alter the structure of actin monomers.

Actinin↗
PubMed1981

Effect of alpha-actinin on actin structure: viscosity studies.

The effect of ATP on ability of alpha-actinin to increase viscosity of F-actin was measured in three different solutions: 100 mM KCl; 100 mM KCl/l mM Mg2+; and Mg2+ alone at concentrations of 1-6 mM. When ATP and Mg2+ are added at equimolar ratios or at added [ATP] to added [Mg2+] greater than equimolar, alpha-actinin has no effect on F-actin viscosity in the absence of KCl. ATP decreases viscosity of alpha-actinin/F-actin mixtures by 20% even in the presence of KCl, evidently because ATP affects the alpha-actinin-F-actin interaction. Molar ratios of 1 alpha-actinin to 49 actins increase specific viscosity of F-actin approx. 2-fold at 37 degrees C in the presence of 1 mM ATP, so ATP does not prevent the alpha-actinin-F-actin interaction.

Actinin↗
PubMed1981

Levels and syntheses of cerebrosides and sulfatides in subcellular fractions of jimpy mutants.

During the period of brain development, the levels of nonhydroxy- and hydroxycerebrosides in the cytosol from brains of jimpy mutants were determined by high-performance liquid chromatography and compared to those in the rest of the particulates from the same brains as well as those in the littermate controls. The concentrations of cerebrosides in jimpy brain preparations were much lower than in controls at all ages. In another experiment, [U-14C]glucose was injected intraperitoneally into jimpy mutants and their littermate controls. The amounts of radioactivity incorporated into cerebrosides and sulfatides in brain cytosol, the microsome-rich fraction, and the rest of the heavier particles were determined. Although the total radioactivity incorporated into these lipids was much lower in jimpy, the specific activities were 2-3 times the control value in all subcellular fractions.

Animals↗