Insulin-like growth factor-I binding proteins in serum from the domestic fowl
| Autor: | C. Goddard, D. G. Armstrong, C. O. McKay, D. J. Morrell |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
medicine.medical_specialty
Endocrinology Diabetes and Metabolism Fowl Peptide Biology DNA-binding protein Gel permeation chromatography Endocrinology Somatomedins Internal medicine medicine Animals Insulin-Like Growth Factor I Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid chemistry.chemical_classification Binding Sites Binding protein biology.organism_classification Insulin-Like Growth Factor Binding Proteins Biochemistry chemistry Electrophoresis Polyacrylamide Gel Insulin-like growth factor I binding Carrier Proteins Quantitative analysis (chemistry) Chickens |
| Zdroj: | The Journal of endocrinology. 120(3) |
| ISSN: | 0022-0795 |
| Popis: | This investigation describes the presence of insulinlike growth factor-I (IGF-I) binding proteins in chicken serum. Whole blood was collected from broiler chickens of 7–9 weeks of age and analysed for binding proteins after gel permeation chromatography under both neutral and acidic conditions, and by polyacrylamide gel electrophoresis in the presence of 12·5% sodium dodecyl sulphate (SDS-PAGE). When serum was chromatographed under neutral conditions, about 70% of the IGF-I immunoreactivity was associated with a large protein complex (Mr=150 000) and 20–25% was associated with an intermediate-sized protein complex (Mr = 45 000). Up to 6% of the serum IGF-I immunoreactivity was eluted in a fraction which corresponded to an Mr of about 7500 and was presumably free IGF-I. Chromatography under acidic conditions dissociated the IGF-I/protein complexes and revealed the presence of an acid-stable binding protein (Mr = 50 000–60 000). After analysis of serum by SDS-PAGE, three monomeric IGF-I binding proteins (Mr = 28 800, 33 200 and 40 700) were detected. The largest monomer (Mr = 40 700) is probably the binding protein component of the intermediate-sized IGF-I/protein complex. The relationship between the other monomers and both the large IGF-I/protein complex and the acid-stable binding protein is not known. Although the pattern of binding proteins in chicken serum is similar to that observed in mammals, a major difference is the presence of up to 6% of the serum IGF-I immunoreactivity in an unbound form. Journal of Endocrinology (1989) 120, 373–378 |
| Databáze: | OpenAIRE |
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