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Related Experiment Videos

High-affinity binding of melatonin to hemoglobin

E Gilad1, N Zisapel

  • 1Department of Biochemistry, Tel Aviv University, Israel.

Biochemical and Molecular Medicine
|December 1, 1995
PubMed
Summary

Hemoglobin interferes with melatonin measurements by binding to the hormone and tracer. This binding is specific and may indicate hemoglobin acts as a carrier protein for melatonin in the bloodstream.

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Area of Science:

  • Biochemistry
  • Endocrinology
  • Analytical Chemistry

Background:

  • Melatonin measurements in hemolyzed blood are often inaccurate.
  • Hemoglobin's potential interaction with melatonin and radioimmunoassay tracers is not well understood.

Purpose of the Study:

  • To investigate the binding of melatonin and its iodinated tracer (125I-melatonin) to hemoglobin.
  • To determine if hemoglobin interferes with melatonin assays and understand the mechanism of interaction.

Main Methods:

  • Purified bovine hemoglobin was used to study the specific binding of 125I-melatonin.
  • Binding kinetics (Kd, Bmax) were determined.
  • Inhibition studies were performed using melatonin analogs, guanine nucleotides, sodium cyanide, and 2,3-bisphosphoglycerate.

Main Results:

  • 125I-melatonin binding to hemoglobin was rapid, saturable, reversible, and inhibited by melatonin and related compounds.
  • Binding was not affected by guanine nucleotides or sodium cyanide, indicating it's not receptor-mediated or heme-related.
  • 2,3-bisphosphoglycerate reduced binding affinity and capacity, suggesting conformation-specific binding in oxyhemoglobin.

Conclusions:

  • Hemoglobin can interfere with melatonin determination assays by competing with the tracer.
  • Hemoglobin may function as a carrier protein for melatonin, potentially enhancing its delivery and efficacy in target tissues.

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