Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures.

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Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
MyeloperoxidaseP05164Details