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Biologically active peptides of casein and lactotransferrin implicated in platelet function
A M Fiat1, S Levy-Toledano, J P Caen
1Laboratoire des Protéines UA CNRS 1188, Université de Paris V, France.
The Journal of Dairy Research
|January 1, 1989
Summary
Milk proteins in colostrum contain biologically active peptides that impact platelet function. These peptides inhibit platelet aggregation and fibrinogen binding, similar to blood-clotting factors.
Area of Science:
- Biochemistry
- Hematology
- Nutritional Science
Background:
- Maternal colostrum and milk are crucial early nutrition sources for newborns.
- Milk proteins, particularly casein and lactotransferrin, are recognized for their nutritional value.
- Emerging research suggests milk proteins may possess bioactive properties beyond nutrition.
Purpose of the Study:
- To investigate the potential of milk-derived peptides from casein and lactotransferrin.
- To determine the effect of these peptides on platelet aggregation and function.
- To compare the activity of milk peptides with known fibrinogen peptides.
Main Methods:
- Isolation of peptides from casein and lactotransferrin.
- In vitro assays to assess platelet aggregation induced by adenosine diphosphate (ADP).
- Measurement of [125I]fibrinogen binding to ADP-treated platelets.
Main Results:
- Peptides isolated from casein and lactotransferrin demonstrated activity on platelet function.
- These milk-derived peptides significantly inhibited ADP-induced platelet aggregation.
- The peptides also reduced the binding of [125I]fibrinogen to ADP-treated platelets.
- Observed effects were comparable to those of fibrinogen peptides.
Conclusions:
- Milk proteins in colostrum and milk yield biologically active peptides.
- These peptides possess anti-platelet activity, inhibiting aggregation and fibrinogen binding.
- Milk proteins share functional similarities with blood-clotting phenomena, suggesting a dual role in infant physiology.