Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures.
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.
Yamada
M
M
Institute for Protein Research, Osaka University, Japan.
Hur
S J
SJ
Toda
H
H
D000595:Amino Acid Sequence; D004792:Enzyme Precursors / Q000302:isolation & purification*; D005110:Extracellular Space / Q000201:enzymology; D006801:Humans; D007951:Leukemia, Myeloid / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009195:Peroxidase / Q000378:metabolism*; D011233:Precipitin Tests; D013057:Spectrum Analysis; D014407:Tumor Cells, Cultured
D004792:Enzyme Precursors; D009195:Peroxidase