Proteolytic degradation routes for turkey beta 1-adrenoceptor probed with antipeptide antibodies against the N-terminal sequence of the receptor |
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Authors: | F G Dunkel G Münch F Boege R Cantrill N P Kurstjens |
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Institution: | Department of Physiological Chemistry, University of Würzburg, Medical School, Federal Republic of Germany. |
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Abstract: | 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. |
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