Proteolytic degradation routes for turkey beta 1-adrenoceptor probed with antipeptide antibodies against the N-terminal sequence of the receptor.
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.
Dunkel
F G
FG
Department of Physiological Chemistry, University of Würzburg, Medical School, Federal Republic of Germany.
Münch
G
G
Boege
F
F
Cantrill
R
R
Kurstjens
N P
NP
D000345:Affinity Labels / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex / Q000032:analysis*; D001386:Azides / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D010869:Pindolol / Q000031:analogs & derivatives / Q000378:metabolism; D011943:Receptors, Adrenergic, beta / Q000302:isolation & purification / Q000378:metabolism*; D014422:Turkeys
D000345:Affinity Labels; D000906:Antibodies; D000936:Antigen-Antibody Complex; D001386:Azides; D010446:Peptide Fragments; D011943:Receptors, Adrenergic, beta; C061987:cyanopindolol azide-2; D010869:Pindolol