Immunoblot studies of the IGF-related acid-labile subunit
| Autor: | David R. Powell, R. P. Diaugustine, Aruna Khare, Raymond L. Hintz, Phillip D.K. Lee, Feng Liu |
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| Rok vydání: | 1994 |
| Předmět: |
medicine.medical_specialty
Glycosylation Macromolecular Substances Endocrinology Diabetes and Metabolism Protein subunit Immunoblotting Clinical Biochemistry Biology Biochemistry Insulin-like growth factor-binding protein chemistry.chemical_compound Endocrinology Antibody Specificity Insulin-Like Growth Factor II Pregnancy Internal medicine medicine Animals Humans Ternary complex Glycoproteins Antiserum chemistry.chemical_classification Immune Sera Biochemistry (medical) Hydrogen-Ion Concentration Insulin-Like Growth Factor Binding Proteins Molecular Weight Postmenopause Somatropin Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase chemistry Growth Hormone Insulin-like growth factor 2 Acromegaly biology.protein Female Carrier Proteins Glycoprotein |
| Zdroj: | The Journal of Clinical Endocrinology & Metabolism. 79:1883-1886 |
| ISSN: | 1945-7197 0021-972X |
| DOI: | 10.1210/jcem.79.6.7527417 |
| Popis: | Insulin-like growth factors I and II (IGF-I and II) are present in serum primarily within a ternary complex consisting of IGF, IGF-binding protein-3 (IGF-3) and acid-labile subunit (ALS). Relatively little is known about ALS as compared to the other components of the complex. We report immunoblot studies of ALS using a new rabbit antiserum to human ALS1-34. The antiserum shows high specificity for ALS, labelling only the intact 82-88 kDa doublet in whole serum. Treatment with endoglycosidase-F leads to only a partial deglycosylation of ALS in whole serum, while purified ALS is reduced to M(r) approximately 58 kDa. Acidification of both whole serum and purified ALS leads to a complete loss of ALS ability to bind to cross-linked IGFBP-3:[125I]IGF-II tracer; however, immunoblot studies show no change in the apparent M(r) of the major ALS band. Immunoblot studies of human serum shows that intact ALS is decreased in growth-hormone (GH) deficiency, increases with GH treatment, is elevated in GH excess and is unchanged with IGF-I treatment. These data provide new information regarding the characteristics of ALS and demonstrate the research utility of a highly-specific antiserum for this protein. |
| Databáze: | OpenAIRE |
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