Sequence homology in the metalloproteins; purple acid phosphatase from beef spleen and uteroferrin from porcine uterus.
The primary structures of purple acid phosphatase and uteroferrin, two iron-binding glycoproteins isolated from beef spleen and porcine uterine fluids, respectively, have been examined by a combination of tandem mass spectrometry and classical Edman sequencing methods. Reported here are amino acid sequence data covering more than 90% of the primary structures for these two proteins. The sequence data reveal an unexpectedly high degree of homology, greater than 90%, for these two proteins.
D000135:Acid Phosphatase / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D005260:Female; D007527:Isoenzymes; D013058:Mass Spectrometry; D008667:Metalloproteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013154:Spleen / Q000201:enzymology*; D013552:Swine; D000071681:Tartrate-Resistant Acid Phosphatase; D014599:Uterus / Q000378:metabolism*
D007527:Isoenzymes; D008667:Metalloproteins; D000135:Acid Phosphatase; D000071681:Tartrate-Resistant Acid Phosphatase