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The complete amino acid sequence of bovine milk angiogenin
Author(s) -
Maes P.,
Damart D.,
Rommens C.,
Montreuil J.,
Spik G.,
Tartar A.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81027-5
Subject(s) - angiogenin , rnase p , peptide sequence , biochemistry , protein sequencing , amino acid , ribonuclease , chemistry , pancreatic ribonuclease , sequence (biology) , biology , genetics , rna , gene , angiogenesis
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.