the binding was highly specific for et-1 , because ( 1 ) none of the other various peptides or ca2+-channel antagonists affected the binding , ( 2 ) the scission of disulfide bonds , the digestion of the c-terminal 6-amino acid residues , or nitrophenylsulfenylization of the c-terminal trp21 of et-1 markedly reduced the binding ability and , ( 3 ) et-1 showed the highest affinity for the vascular receptor among three et isopeptides .
C0079281
et-1
C0079284
et