Immunologic Studies of Adrenocorticotropic Hormone (ACTH): Effect of Carboxypeptidase Digestion on Biologic and Immunologic Activities
| Autor: | Satoshi Hane, Gerold M. Grodsky, Misako Tosaka, Peter H. Forsham, Lowell L. Sparks, Hiroo Imura |
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| Rok vydání: | 1967 |
| Předmět: |
endocrine system
medicine.medical_specialty Phenylalanine Endocrinology Diabetes and Metabolism Clinical Biochemistry Carboxypeptidases Adrenocorticotropic hormone Biochemistry Endocrinology Adrenocorticotropic Hormone Glutamates Leucine Internal medicine medicine Animals Humans Immunoassay chemistry.chemical_classification Sheep biology Chemistry Immune Sera Biochemistry (medical) Glutamic acid Carboxypeptidase Amino acid Antibody Formation biology.protein Biological Assay Cattle Chromatography Thin Layer hormones hormone substitutes and hormone antagonists |
| Zdroj: | The Journal of Clinical Endocrinology & Metabolism. 27:15-21 |
| ISSN: | 1945-7197 0021-972X |
| DOI: | 10.1210/jcem-27-1-15 |
| Popis: | The radioimmunologic activity of ovine ACTH (αs-ACTH) and a C-terminal (αs22–39-ACTH) fraction of ovine ACTH before and after carboxypeptidase digestion was studied with 2 antiporcine and 2 antiovine ACTH sera. The amino acids released after carboxypeptidase digestion were measured. These were mainly the C-terminal phenylalanine and only traces of glutamic acid and leucine. With the 2 antiporcine ACTH sera, the immunologic activity of αs-ACTH and αs22–39-ACTH was almost completely abolished by carboxypeptidase treatment. The steroidogenic activity of ACTH was unchanged. This is a further example of the dissociation in immunologic and biologic activities of ACTH. With 2 antiovine ACTH sera, the results were different: carboxypeptidase treatment caused only a slight decrease in immunologic activity of αs-ACTH but a marked decrease in that of αs22–39-ACTH. It is concluded that the C-terminal phenylalanine is necessary for the binding of ACTH peptides with the antiporcine ACTH sera studied. While the... |
| Databáze: | OpenAIRE |
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