The molecular size of angiotensin II (A II) receptor, whose previous estimates are of uncertain validity, has been established by partial purification and affinity labeling. A II receptors were solubilized from bovine adrenal cortex with 3[(3-cholamidopropyl)dimethylamino]-l-propanesulfonate and partially purified by ion exchange chromatography on DEAE-Toyopearl, hydrophobic chromatography on phenyl-Sepharose, and affinity chromatography on wheat germ lectin-Sepharose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified material revealed that 130,000-170,000 M, species were highly enriched and showed a good correlation with the activity profiles. Affinity labeling experiments showed that 'Z51-AII-receptor complexes, cross-linked with disuccinimidyl suberate, have a M, ofabout 170,000. These results indicate that the A II receptor is a glycoprotein of about 170 kDa.
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Akiyama et al. (1986) studied this question.