Tritosol: A new scintillation cocktail based on Triton X-100

Fricke, Uwe

doi:10.1016/0003-2697(75)90379-6

Cited by 385 publications

(101 citation statements)

References 4 publications

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“…Then 5 ml of chloroform and 4 ml of 0.01 M H2SO ~ were added and the mixture was sonicared and centrifuged as above. A 1 ml sample (2 ml for hydrolysates) of the aqueous (upper) phase was removed for liquid scintillation counting in 10 ml of a xylene based scintillant (Fricke 1975). A further 1 ml aliquot (20 gl for hydrolysates) was analyzed for PEA concentration according to Suzuki and Yagi (1976).…”

Section: Methodsmentioning

confidence: 99%

Protein metabolism in the pectoralis muscle and liver of hibernating bats,Eptesicus fuscus

Yacoe

1983

J Comp Physiol B

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Summary. Seasonal variations in protein metabolism of the pectoralis muscle and liver of the big brown bat, Eptesicus fuscus, are examined in relation to seasonal changes in physiological status. A technique is described for the determination of protein synthetic rates in vivo in animals too small for conventional methods. The results indicate no detectable rates of protein synthesis in hibernating bats during torpor bouts ( Table 2). Rates of synthesis in hibernating bats during periods of arousal are comparable to those of active summer bats (Table 2), despite the fact that the hibernating bats had not eaten in over 2 months. Rates of protein degradation were calculated from the rate of urea formation in torpid bats (Figs. 4, 5), the overall loss of pectoralis muscle and liver protein mass during hibernation (Table 3), the proportion of the total time of hibernation spent in torpor and arousal (Table 1), and the observed rates of protein synthesis (Table 2). These estimates (Table 4) indicate negligible rates of protein degradation in torpid bats. However, protein degradation during periodic arousals is comparable to that of summer bats after an overnight fast. These findings are consistent with earlier observations suggesting that significant gluconeogenesis from tissue protein occurs during spontaneous arousals from hibernation.

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Section: Methodsmentioning

confidence: 99%

Protein metabolism in the pectoralis muscle and liver of hibernating bats,Eptesicus fuscus

Yacoe

1983

J Comp Physiol B

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“…Cotyledons were ground gently with buffer in a mortar and pestle, and chloroplasts were isolated by differential centrifugation. Chloroplasts were disrupted by sonication in hypotonic buffer (10 mm Tris-HCl [pH 7.5], 10 mm Mg(acetate)2, 500 mM NaCl, 10 mm ,8-mercaptoethanol), then low mol wt RNA was isolated from a high-speed supernatant as described above for algal extracts.…”

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confidence: 99%

Stimulation of δ-Aminolevulinic Acid Formation in Algal Extracts by Heterologous RNA

Weinstein¹,

Mayer²,

Beale³

1986

Plant Physiol.

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Formation of the chlorophyll and heme precursor &.aminolevulinic acid (ALA) from glutamate in soluble extracts of Chlorella vulgaris, Euglena grailis, and Cyanidium caldanium was stimulated by addition of low molecular weight RNA derived from greening algae or plant tissue. Enzyme extracts were prepared for the ALA formation assay by highspeed centrifugation, partial RNA depletion, and gel filtration through Sephadex G-25. RNA was extracted from greening barley epicotyls, greening cucumber cotyledon chloroplasts, and growing cells of Chlorella, Euglena, Chlamydomonas reinhardtii, and Anacystis nidulans, freed of protein, and fractionated on DEAE-cellulose to yield an active component corresponding to the tRNA-containing fraction. RNA from homologous and heterologous species stimulated ALA formation when added to enzyme extracts, and the degree of stimulation was proportional to the amount of RNA added. Algal enzyme extracts were stimulated by alpl RNAs interchangeably, with the exception of RNA prepared from aplastidic Euglena, which did not stimulate ALA production. RNA from greening cucumber cotyledon chloroplasts and greening barley epicotyls stimulated ALA formation in algal enzyme incubations. In contrast, tRNA from Escherichia coli, both nonspecific and glutamate-specific, as well as wheat germ, bovine liver, and yeast tRNA, failed to reconstitute ALA formation. Moreover, E. coli tRNA inhibited ALA formation by algal extracts, both in the presence and absence of added algal RNA. Chlorella extracts were capable of catalyzing aminoacyl bond formation between glutamate and both the activity reconstituting and nonreconstituting RNAs, indicating that the inability of some RNAs to stimulate ALA formation was not due to their inability to serve as glutamyl acceptors. The first step in the ALA-forming reaction sequence has been proposed to be activation of glutamate via aminoacyl bond formation with a specific tRNA, analogous to the first step in peptide bond formation. Our results suggest that the RNA that is required for ALA formation may be functionally distinct from the glutamyl-tRNA species involved in protein synthesis.The formation of ALA3 is the first committed step in the tetrapyrrole biosynthetic pathway leading to hemes, Chls, and bilins. In plants and algae, most, and possibly all, ALA is formed via a 5-carbon pathway which utilizes the intact carbon skeleton '

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“…The uptake process was initiated by the addition of L-[3-4 3 H]glutamate, to give a final concentration of 1.0 M (specific activity: 1nCi/pmol) and was interrupted after 3 min by dilution with 10 ml of cold (0 Њ C) radioactive Krebs-Tris medium followed by filtration under vacuum on Millipore (DAWP; .65 mm). The filters were washed 3 times with 10 ml cold Krebs-Tris medium and dropped into scintillation vials where the radioactivity was measured after the addition of 10 ml Tritosol (Fricke 1975). Blanks were prepared by incubating the preparation used with [ 3 H]glutamate at 0 Њ C.…”

Section: Amino Acid Analysismentioning

confidence: 99%

The Vigilance Promoting Drug Modafinil Increases Extracellular Glutamate Levels in the Medial Preoptic Area and the Posterior Hypothalamus of the Conscious Rat Prevention by Local GABAA Receptor Blockade

Ferraro

1999

Neuropsychopharmacology

141

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Tritosol: A new scintillation cocktail based on Triton X-100

Cited by 385 publications

References 4 publications

Protein metabolism in the pectoralis muscle and liver of hibernating bats,Eptesicus fuscus

Protein metabolism in the pectoralis muscle and liver of hibernating bats,Eptesicus fuscus

Stimulation of δ-Aminolevulinic Acid Formation in Algal Extracts by Heterologous RNA

The Vigilance Promoting Drug Modafinil Increases Extracellular Glutamate Levels in the Medial Preoptic Area and the Posterior Hypothalamus of the Conscious Rat Prevention by Local GABAA Receptor Blockade

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