Abstract
1. 1. An acid-stable IGF binding protein was isolated and purified from porcine serum. 2. 2. The protein comprised two major species with Mrs of 45 and 41 kDa determined using SDS-PAGE under reducing conditions. 3. 3. The IGFBP preparation specifically bound both IGF-I and II. 4. 4. Four distinct protein bands (Mrs of 23, 45, 50 and 75 kDa) in the porcine IGFBP preparation specifically bound radiolabelled IGF-I. 5. 5. The porcine IGFBP exhibited sequence homology with IGFBPs from human plasma and rat serum. 6. 6. This is the first report of the purification and characterization of the acid-stable IGFBP from porcine serum.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 561-567 |
| Number of pages | 7 |
| Journal | Comparative biochemistry and physiology. B, Comparative biochemistry |
| Volume | 92 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1989 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Physiology
- Molecular Biology
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