Abstract
Synthetic peptides corresponding to the C-terminal region of angiogenin (Ang) inhibit the enzymatic and biological activities of the molecule while peptides from the N-terminal region do not affect either activity. The peptide Ang(108–121) transiently abolishes the inhibition of cell-free protein synthesis caused by angiogenin coincidentally with its cleavage of reticulocyte RNA. Several C-terminal peptides also inhibit nuclease activity of angiogenin when tRNA is the substrate. Furthermore, peptide Ang(108–123) significantly decreases neovascularization elicited by angiogenin in the chick chorioallantoic membrane assay.
Published Version
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