Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures.
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Yamada M, Hur SJ, Toda H
Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures.
Biochem Biophys Res Commun. 1990 Jan 30;166(2):852-9.
- PubMed ID
- 2154223 [ View in PubMed]
- Abstract
An extracellular myeloperoxidase precursor of HL-60 cells was purified from the culture supernatant by ammonium sulfate precipitation, DEAE-Sepharose chromatography, and monoclonal antibody affinity chromatography. The purified protein was a glycoprotein of approximately 89 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The amino-terminal amino acid sequence of the protein began at amino acid residue 49 of the 745-amino acid sequence deduced from a myeloperoxidase cDNA, suggesting that the protein consisted of 697 amino acid residues. The implications of the precursor in the processing of myeloperoxidase are discussed.