Paper
An improved method excluding hemoglobin interferences for lysosomal hydrolase assays using colorimetric synthetic substrates, 2-(N-hexadecanoylamino)-4-nitrophenol derivatives.
Published Apr 15, 1983 · T. Levade, R. Salvayre, J. Sicre
Analytical biochemistry
Q3 SJR score
5
Citations
0
Influential Citations
Abstract
Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.
Study Snapshot
Selective extraction of 2-(N-hexadecanoylamino)-4-nitrophenol allows for lysosomal hydrolase assays without hemoglobin interference, enabling sphingomyelin phosphodiesterase, glucosylceramidase, and galact
PopulationOlder adults (50-71 years)
Sample size24
MethodsObservational
OutcomesBody Mass Index projections
ResultsSocial networks mitigate obesity in older groups.
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References
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Citations
A comprehensive review on designing nanocomposite adsorbents for efficient removal of 4-nitrophenol from water
Nanocomposite adsorbents show potential for efficient removal of 4-nitrophenol from water, with potential for large-scale decontamination and environmental acceptance.
2024·15citations·N. El Messaoudi et al.·Nano-Structures & Nano-Objects
Nano-Structures & Nano-Objects
A Novel High-Throughput Screening Format to Identify Inhibitors of Secreted Acid Sphingomyelinase
A novel high-throughput screening format identified novel compounds that inhibit secreted acid sphingomyelinase at pH 7.4, with both organic and bead-based extraction methods showing similar results and adaptability to 384-well format.
2005·14citations·R. Mintzer et al.·Journal of Biomolecular Screening
Journal of Biomolecular Screening
Hexachlorobenzene-induced alterations on neutral and acidic sphingomyelinases and serine palmitoyltransferase activities. A time course study in two strains of rats.
Hexachlorobenzene-induced decrease in hepatic sphingomyelin content may serve as a protective mechanism against liver injury, but strain-dependent.
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Molecular forms of sphingomyelinase and non-specific phosphodiesterases in Epstein-Barr virus-transformed lymphoid cell lines from Niemann-Pick disease types A and B.
In lymphoid cell lines, sphingomyelinase and phosphodiesterases have separate genetic coding, and their activities are not reliable for diagnosing Niemann-Pick disease.
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Sphingomyelinase and nonspecific phosphodiesterase activities in Epstein-Barr virus-transformed lymphoid cell lines from Niemann-Pick disease A, B and C.
Deficient acid sphingomyelinase activity is found in Epstein-Barr virus-transformed lymphoid cell lines from Niemann-Pick disease types A and B, but not in those from type C and sea-blue histiocyte syndrome.
1984·16citations·T. Levade et al.·Biochimica et biophysica acta
Biochimica et biophysica acta