The complete amino acid sequence of bovine milk angiogenin

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Abstract
The amino acid sequence of angiogenin isolated from bovine milk was deduced by gas‐phase sequencing of the protein and its fragments. The protein contains 125 residues and has a calculated molecular mass of 14 577 Da. The sequence is highly homologous (65% identity) to the sequence of human angiogenin, most of the differences being the result of conservative replacements. Like human angiogenin, the bovine protein is also homologous to bovine pancreatic RNase A (34% identity) and the three major active site residues known to be involved in the catalytic process, His‐14, Lys‐41 and His‐115, are conserved. When tested against conventional substrates for RNase A activity, bovine angiogenin displays the same selective ribonucleolytic activity as human angiogenin. The sequence of bovine angiogenin contains the cell recognition tripeptide Arg‐Gly‐Asp which is not present in the human protein.