ABSTRACT
Immunoreactive insulin-like growth factor-I (IGF-I) in bovine milk was quantified. IGF-I was principally association with an ∼45 kDa binding protein. In addition, a small fraction of IGF-I occurred at a molecular weight approximately the same as that of unbound IGF-I. Available binding sites existed on the ∼45 kDa binding protein. Bound IGF-I was readily dissociated from binding protein by acid treatment. When IGF-I was estimated in milk obtained from primiparous and multiparous cows, multiparous cows had a higher concentration (40 μmol/l) at parturition than primiparous cows (19·2 μmol/l). By day 2 of lactation, IGF-I concentrations were 30 and 50% of initial estimates for multiparous and primiparous cows respectively. The final IGF-I concentration, on day 56 of lactation, was 4·5 μmol/l for combined parity groups. At parturition in multiparous cows, the mass of IGF-I was estimated at 183 and 157 μmol for blood and milk pools respectively. Milk, therefore, represents a substantial pool of IGF-I in the cow. The mechanism of the appearance of IGF-I in bovine milk is unknown.
Journal of Endocrinology (1989) 120, 21–29
Autoradiographic Localization of Insulin-Like Growth Factor I Binding Sites in the Bovine Adrenal Gland and on Cultured Bovine Adrenal Chromaffin Cells
