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- W2093660130 abstract "Anti-peptide antibodies, raised against the N-terminal sequence (amino acids 2–10) of the turkey β1-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 [Jürß, 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." @default.
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- W2093660130 date "1989-11-01" @default.
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- W2093660130 title "Proteolytic degradation routes for turkey β1-adrenoceptor probed with antipeptide antibodies against the N-terminal sequence of the receptor" @default.
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- W2093660130 doi "https://doi.org/10.1016/0006-291x(89)91064-4" @default.
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