Abstract
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.
MeSH Terms
Adrenal Glands/metabolism
Angiotensin II/analogs & derivatives,metabolism
Angiotensin III/metabolism
Animals
Kinetics
Rats
Receptors, Angiotensin/metabolism
Receptors, Cell Surface/metabolism
Chemicals
Receptors, Angiotensin
Receptors, Cell Surface
Angiotensin II
Angiotensin III
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Devynck M A
Pernollet M G
Matthews P G
Khosla M C
Bumpus F M
Meyer P
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