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Epidermal growth factor reactivity in rat milk.
Regulatory Peptides
|September 10, 1990
Summary
Epidermal Growth Factor (EGF) levels in rat whey increase during lactation. Rat whey EGF is a larger 80 kDa form, not derived from salivary glands, and differs from the smaller 6 kDa EGF.
Area of Science:
- Biochemistry
- Developmental Biology
- Lactation Biology
Background:
- Epidermal Growth Factor (EGF) is crucial for cell growth and development.
- EGF's presence and form in lactational secretions are not fully characterized.
- Investigating EGF in rat whey provides insights into its role during neonatal development.
Purpose of the Study:
- To characterize the concentration, molecular form, and origin of EGF in rat whey.
- To compare rat whey EGF with salivary gland EGF.
- To understand the stability and potential binding proteins of EGF in rat milk.
Main Methods:
- Quantification of EGF immunoreactivity in rat whey across lactation.
- Gel chromatography (S-200) and gel filtration to determine molecular weight and size.
- Immuno-affinity chromatography for partial purification.
- Binding studies using radiolabeled EGF and antibodies.
- Incubation of rat milk to assess EGF stability.
Main Results:
- EGF concentration in rat whey significantly increases from lactation day 1 to day 19.
- The predominant form of EGF in whey is an 80 kDa complex, not the 6 kDa free form.
- Sialoadenectomy did not affect whey EGF levels, and whey lacked EGF binding proteins.
- Incubation of milk degraded the 80 kDa form into 35 kDa and 6 kDa forms.
- Whey EGF showed different antibody binding compared to submandibular EGF but similar receptor binding.
Conclusions:
- EGF in rat whey exists primarily as a large complex (80 kDa) that changes during lactation.
- This whey EGF is unlikely to originate from the submandibular salivary glands.
- The 80 kDa complex is unstable and can be degraded into smaller forms in rat milk.