Recognition of insulin-like growth factor (IGF) serum binding proteins by an antibody raised against a specific IGF-inhibitor
Evidence suggests that a specific inhibitor of the insulin-like growth factors (IGF) which acts by binding to IGF may be structurally related to the native, MW 150K binding protein (BP) in serum. This has now been examined using a polyclonal antiserum (R8) raised against highly purified inhibitor. Western blotting analysis of inhibitor using R8 gave 4 immunoreactive (ir-) bands (MW 34.5K, 23K, 16K and 12K), the most intense being the MW 16K band, identical to the MW of the inhibitor. Ligand blotting using /sup 125/I-IGF-I indicated specific IGF-binding activity at MW 29K, 26.5K, 16K and 12K, indicating that at least 2 of the ir-bands (16K and 12K) were IGF-BPs. Western blotting of a salt-precipitated fraction of serum gave 8 ir-bands of which 3 (MW 42K, 38K and 34K) were identical with BP bands detected previously by Hossenlopp et al. These immunological crossreactivities indicate that the inhibitor is structurally related to the higher MW IGF-BPs in serum.
- Research Organization:
- Prince Henry's Hospital, Melbourne (Australia)
- OSTI ID:
- 6603195
- Journal Information:
- Biochem. Biophys. Res. Commun.; (United States), Vol. 156:2
- Country of Publication:
- United States
- Language:
- English
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MOLECULAR WEIGHT
PRECIPITATION
TRACER TECHNIQUES
BETA DECAY RADIOISOTOPES
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550201* - Biochemistry- Tracer Techniques