Abstract:
:125I-labelled angiotensin II (A II) specifically binds to solubilized receptors extracted from rat isolated glomeruli using CHAPS (3-[3-( cholamidopropyl ) dimethylammonio ]-1-propanesulfonate). The yield of solubilization of the binding sites was 3.3%. Equilibrium was reached after 15-20 min and specific binding represented 75% of total binding. Dissociation of the hormone-receptor complex after addition of an excess of A II was very slow in the presence of Ca2+ and Mg2+. [Sar1 Ala8] A II and [Sar1 Ile8] A II were more potent as competitive inhibitors of 125I-labelled A II than A II itself and its heptapeptide. These basic features of 125I-labelled A II binding to the extracted material were similar to those observed previously with untreated glomeruli.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chansel D,Ardaillou N,Ardaillou Rdoi
10.1016/0014-5793(84)81321-6subject
Has Abstractpub_date
1984-05-21 00:00:00pages
243-6issue
2eissn
0014-5793issn
1873-3468journal_volume
170pub_type
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