作者: Hirotoshi Watanabe , Hitoshi Miyazaki , Motohiro Kondoh , Yasushi Masuda , Sadao Kimura
DOI: 10.1016/0006-291X(89)91377-6
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摘要: Abstract Competitive displacement experiments of 125I-endothelin (ET)-1, -2, or -3 binding to chick cardiac membranes were performed with unlabeled ET-1, -3, and sarafotoxin S6b (STX) as competitors. 125I-ET-1 -2 was competitively inhibited by increasing concentrations these peptides in the same order; i.e. ET-2 ≥ ET-1 > ET-3 STX. In contrast, order potency displacing 125I-ET-3 Affinity labeling cross-linking via disuccinimidyl tartarate yielded one major specific band an apparent Mr=53,000 sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed autoradiography. On other hand, affinity showed that two minor bands Mr=34,000, 46,000, 53,000, respectively, specifically labeled. These results indicate presence distinct types ET receptors, which has higher for than is conversely ET-3-preferring.