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Endogenous digitalis-like factors in human milk.
A Clerico1, A Paci, M G Del Chicca
1Istituto di Fisiologia Clinica del CNR, Pisa, Italy.
Clinical Chemistry
|April 1, 1992
Summary
Endogenous digitalis-like factors (EDLFs) are present in human milk and colostrum at concentrations higher than in healthy adults. These factors may play a role in maternal-infant physiology during lactation.
Area of Science:
- Biochemistry
- Endocrinology
- Human Physiology
Background:
- Endogenous digitalis-like factors (EDLFs) are a group of compounds with structural and functional similarities to cardiac glycosides.
- These factors are found in various mammalian tissues and biological fluids, including plasma and breast milk.
Purpose of the Study:
- To quantify the concentration of EDLFs in human milk and colostrum.
- To compare EDLF levels in breast milk with those in healthy adults and pregnant women.
- To investigate the characteristics of EDLFs in milk, including their binding to milk proteins.
Main Methods:
- Measurement of EDLF concentrations using solid-phase radioimmunoassay (RIA) with antidigoxin antibodies.
- Assay of EDLF concentrations using a radioreceptor assay (RRA) involving human placenta Na+/K(+)-ATPase.
- Analysis of milk and serum samples after heating and/or Sep-Pak C18 cartridge extraction.
Main Results:
- Mean EDLF concentrations in milk (35.6 ng/L) and colostrum (61.3 ng/L) were measured by RIA.
- Mean EDLF concentration in milk was 573 ng/L by RRA, with a wide range (0-2098 ng/L).
- EDLF concentrations in milk were higher than in healthy adults but comparable to third-trimester pregnancy serum levels.
- Heating and extraction significantly altered EDLF values in milk and serum.
- EDLFs in milk appeared to be unbound or weakly bound to milk proteins.
Conclusions:
- Human milk and colostrum contain significant concentrations of EDLFs.
- The levels of EDLFs in milk suggest a potential physiological role during lactation.
- EDLFs in milk exhibit different properties compared to serum EDLFs, particularly regarding protein binding.