Immunogenicity and Bioactivity of Glucagon, Modified at Methionine-27
| Autor: | Kempen Hj, Nooijen Wj |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
endocrine system
medicine.medical_specialty Swine Endocrinology Diabetes and Metabolism Clinical Biochemistry Receptors Cell Surface Methylation Biochemistry Glucagon chemistry.chemical_compound Endocrinology Internal medicine medicine Animals Potency Amino Acids Receptor Antiserum Methionine Immunogenicity digestive oral and skin physiology Biochemistry (medical) General Medicine Rats Kinetics Glucose Adipose Tissue chemistry Biological Assay Oxidation-Reduction hormones hormone substitutes and hormone antagonists |
| Zdroj: | Hormone and Metabolic Research. 11:459-463 |
| ISSN: | 1439-4286 0018-5043 |
| DOI: | 10.1055/s-0028-1092761 |
| Popis: | Porcine glucagon was modified at methionine-27 by methylation or oxidation. Antisera against the glucagon derivatives were obtained. One of these antisera showed a high affinity for glucagon, with no cross-reactivity with gut-GLI 1. Biological activities of these derivatives were assessed on rat hepatocytes. Both derivatives had the same maximal glucose-mobilising activity as native glucagon, but a decrease potency, suggesting a crucial role of methionine in the binding of glucagon to its hepatic receptor. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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