Epidermal growth factor reactivity in rat milk
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Epidermal growth factor reactivity in rat milk. / Raaberg, Lasse; Nexø, Ebba; Tollund, L; Poulsen, Steen Seier.
I: Regulatory Peptides, Bind 30, Nr. 2, 10.09.1990, s. 149-57.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Epidermal growth factor reactivity in rat milk
AU - Raaberg, Lasse
AU - Nexø, Ebba
AU - Tollund, L
AU - Poulsen, Steen Seier
PY - 1990/9/10
Y1 - 1990/9/10
N2 - The concentration of EGF immunoreactivity in rat whey increases from 0.3 pmol/ml at lactation day 1 to 2.0 pmol/ml at lactation day 19. The concentration of EGF is not influenced when the rats undergo sialoadenectomy prior to mating. On S-200 gel chromatography, almost all EGF-reactivity in rat whey elutes as a broad peak corresponding to a Stokes radius of 4.0 nm (an approximate molecular weight of 80 kDa). Almost no 6 kDa EGF is present. Judged by gel filtration of whey pre-incubated with 125I-EGF (6 kDa), no binding protein for EGF is present in rat whey. When rat milk is incubated overnight at 37 degrees C, the 80 kDa EGF is degraded and elutes as a peak with a Stokes radius of 2.7 nm, corresponding to a molecular weight of approximately 35 kDa EGF and as a peak corresponding to 6 kDa EGF. Also, after partial purification by immuno-affinity chromatography, the EGF-reactive material in rat whey behaves as a peptide with a Stokes radius of 2.7 nm, corresponding to a molecular weight of approximately 35 kDa at gel filtration. Comparative binding studies between EGF purified from the submandibular glands and the EGF purified from rat whey confirm differences in the binding to antibodies raised against submandibular EGF, but not in binding to the EGF-receptor. Our results make it unlikely that EGF in rat whey is derived from the submandibular glands.
AB - The concentration of EGF immunoreactivity in rat whey increases from 0.3 pmol/ml at lactation day 1 to 2.0 pmol/ml at lactation day 19. The concentration of EGF is not influenced when the rats undergo sialoadenectomy prior to mating. On S-200 gel chromatography, almost all EGF-reactivity in rat whey elutes as a broad peak corresponding to a Stokes radius of 4.0 nm (an approximate molecular weight of 80 kDa). Almost no 6 kDa EGF is present. Judged by gel filtration of whey pre-incubated with 125I-EGF (6 kDa), no binding protein for EGF is present in rat whey. When rat milk is incubated overnight at 37 degrees C, the 80 kDa EGF is degraded and elutes as a peak with a Stokes radius of 2.7 nm, corresponding to a molecular weight of approximately 35 kDa EGF and as a peak corresponding to 6 kDa EGF. Also, after partial purification by immuno-affinity chromatography, the EGF-reactive material in rat whey behaves as a peptide with a Stokes radius of 2.7 nm, corresponding to a molecular weight of approximately 35 kDa at gel filtration. Comparative binding studies between EGF purified from the submandibular glands and the EGF purified from rat whey confirm differences in the binding to antibodies raised against submandibular EGF, but not in binding to the EGF-receptor. Our results make it unlikely that EGF in rat whey is derived from the submandibular glands.
KW - Animals
KW - Chromatography, Gel
KW - Epidermal Growth Factor
KW - Female
KW - Milk
KW - Molecular Weight
KW - Pregnancy
KW - Rats
KW - Rats, Inbred Strains
KW - Receptor, Epidermal Growth Factor
KW - Submandibular Gland
M3 - Journal article
C2 - 2274679
VL - 30
SP - 149
EP - 157
JO - Regulatory Peptides
JF - Regulatory Peptides
SN - 0167-0115
IS - 2
ER -
ID: 47488113