[Interaction of angiotensin analogs and fragments with rat adrenal cell receptors].
The binding of some modified angiotensin (AT) analogs and fragments to isolated rat adrenal glomerular cells was studied by radioreceptor analysis with a view of clarifying the role of C- and N-terminal amino acids in the binding of AT molecules to cell receptors. It was demonstrated that Arg2 and Val3 residues are of great importance for effective binding of the AT molecule to cell receptors. The presence of a free C-terminal carboxylic group in position 8 in the vicinity of the bulky lipophilic residue is a necessary condition for this process. The Asp and Asn residues located in position 1 of the AT molecule are not essential for the binding of the hormone molecule to adrenal cell receptors.
Kublis
G G
GG
Porunkevich
E A
EA
Chipens
G I
GI
D000311:Adrenal Glands / Q000166:cytology / Q000378:metabolism*; D000596:Amino Acids / Q000502:physiology; D000809:Angiotensins / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000502:physiology; D007457:Iodine Radioisotopes; D051381:Rats; D011945:Receptors, Angiotensin / Q000378:metabolism*; D014633:Valine / Q000502:physiology
D000596:Amino Acids; D000809:Angiotensins; D007457:Iodine Radioisotopes; D011945:Receptors, Angiotensin; D001120:Arginine; D014633:Valine
Issledovanie vzaimodeĭstviia analogov i fragmentov angiotenzina s retseptorami kletok nadpochechnikov krys.