
Specific receptors for des-Asp1-angiotensin II (("angiotensin III") in rat adrenals.
Author(s) -
MarieAude Devynck,
Marie-Gabrielle Pernollet,
P. G. Matthews,
M. C. Khosla,
F. M. Bumpus,
Philippe Meyer
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.9.4029
Subject(s) - angiotensin ii , angiotensin iii , dissociation constant , renin–angiotensin system , chemistry , endocrinology , angiotensin receptor , medicine , receptor , angiotensin ii receptor type 1 , aldosterone , biology , biochemistry , blood pressure
The specific binding of angiotensin II and des-Asp1-angiotensin II ("angiotensin III") III") to rat adrenals was studied with the use of the tritiated peptides. The binding sites having maximal affinity for angiotensin II were characterized by an equilibrium dissociation constant of 3.3 to 5.2 X 10(-9) M. Angiotensin III was able to interact with these sites, and also with a class of sites with very high affinity, characterized by an equilibrium dissociation constant of 1 to 2 X 10(-10) M. These sites exhibited a greater affinity for the heptapeptide angiotensin III than for the octapeptide angiotensin II. These findings, together with the known potent aldosterone stimulating effect of angiotensin III and its presence in rat plasma, suggest that this heptapeptide could be the physiologically important steroidogenic angiotensin in this species.