Melatonin-like Immunoreactivity in the Presence of Different Chemicals as Determined by the Radioimmunoassay

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Abstract

To determine the nature of the molecule(s) that is responsible for the melatonin like immunoreactivity (MLI), we measured the effect of pretreatment of plasma samples with detergents, reducing agent, and proteinase K. Nonidet P-40 Triton X-100, and ethylacetate extraction had no effect, while sodium deoxycholate, sodium dodecyl sulfate, β-mercaptoethanol, ether extraction, proteinase K, and temperature increased the MLI. Since the radioimmunoassay (RIA) was sensitive to proteinase K, ionic detergents, and a reducing compound, we hypothesize that a proteinaceous molecule might be responsible for this MLI. We compared our column procedure for RIA of plasma melatonin (1) with procedures involving extraction with either ethylacetate or ether. In our hands preextraction of samples with organic solvents caused a loss of immunoreactivity. We also found that passing samples through the column is more efficient in eliminating interference in the melatonin assay than extracting samples either with ethylacetate or ether.

Original languageEnglish
Pages (from-to)51-54
Number of pages4
JournalBiochemical Medicine and Metabolic Biology
Volume51
Issue number1
DOIs
StatePublished - Feb 1994

Fingerprint

Melatonin
Radioimmunoassay
Endopeptidase K
Ether
Detergents
Plasmas
Molecules
Deoxycholic Acid
Mercaptoethanol
Reducing Agents
Octoxynol
Sodium Dodecyl Sulfate
Organic solvents
Assays
Temperature

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry

Cite this

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abstract = "To determine the nature of the molecule(s) that is responsible for the melatonin like immunoreactivity (MLI), we measured the effect of pretreatment of plasma samples with detergents, reducing agent, and proteinase K. Nonidet P-40 Triton X-100, and ethylacetate extraction had no effect, while sodium deoxycholate, sodium dodecyl sulfate, β-mercaptoethanol, ether extraction, proteinase K, and temperature increased the MLI. Since the radioimmunoassay (RIA) was sensitive to proteinase K, ionic detergents, and a reducing compound, we hypothesize that a proteinaceous molecule might be responsible for this MLI. We compared our column procedure for RIA of plasma melatonin (1) with procedures involving extraction with either ethylacetate or ether. In our hands preextraction of samples with organic solvents caused a loss of immunoreactivity. We also found that passing samples through the column is more efficient in eliminating interference in the melatonin assay than extracting samples either with ethylacetate or ether.",
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AU - Lahiri, Debomoy

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N2 - To determine the nature of the molecule(s) that is responsible for the melatonin like immunoreactivity (MLI), we measured the effect of pretreatment of plasma samples with detergents, reducing agent, and proteinase K. Nonidet P-40 Triton X-100, and ethylacetate extraction had no effect, while sodium deoxycholate, sodium dodecyl sulfate, β-mercaptoethanol, ether extraction, proteinase K, and temperature increased the MLI. Since the radioimmunoassay (RIA) was sensitive to proteinase K, ionic detergents, and a reducing compound, we hypothesize that a proteinaceous molecule might be responsible for this MLI. We compared our column procedure for RIA of plasma melatonin (1) with procedures involving extraction with either ethylacetate or ether. In our hands preextraction of samples with organic solvents caused a loss of immunoreactivity. We also found that passing samples through the column is more efficient in eliminating interference in the melatonin assay than extracting samples either with ethylacetate or ether.

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