Proteolytic degradation routes for turkey β1-adrenoceptor probed with antipeptide antibodies against the N-terminal sequence of the receptor
| Autor: | Nicol P. Kurstjens, Gerald Münch, Richard C. Cantrill, Franz-Georg Dunkel, Fritz Boege |
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| Rok vydání: | 1989 |
| Předmět: |
Azides
Turkeys Proteolysis Immunoblotting Molecular Sequence Data Biophysics Antigen-Antibody Complex Cleavage (embryo) Biochemistry Antibodies chemistry.chemical_compound Receptors Adrenergic beta medicine Animals Amino Acid Sequence Receptor Molecular Biology chemistry.chemical_classification biology medicine.diagnostic_test Erythrocyte Membrane Affinity Labels Cell Biology Molecular biology Peptide Fragments Amino acid Red blood cell EGTA medicine.anatomical_structure chemistry Pindolol biology.protein PMSF Antibody |
| Zdroj: | Biochemical and Biophysical Research Communications. 165:264-270 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(89)91064-4 |
| Popis: | Anti-peptide antibodies, raised against the N-terminal sequence (amino acids 2-10) of the turkey beta 1-adrenoceptor [Yarden et al., Proc. Natl. Acad. Sci. USA (1986) 83, 6795-6799] recognized the 50 kDa- but not the 40 kDa-form of the receptor, thus confirming the previous assumption that the N-terminus of the 50 kDa form is lost during its conversion to the 40 kDa-form [Jür beta, R., Hekman, M.Helmreich, E.J.M. (1985) Biochemistry 24, 3349-3354]. By in situ proteolysis small amounts of receptor fragments were formed, which could be recognized by the N-terminus specific antibody. Therefore, although the production of the stable 40 kDa receptor species by proteolytic removal of a portion of the N-terminal appears to be the predominant route, there exists an additional pathway of degradation which must involve the initial cleavage of the carboxyl terminal. |
| Databáze: | OpenAIRE |
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