Yamada M, Hur S J, Toda H
Institute for Protein Research, Osaka University, Japan.
Biochem Biophys Res Commun. 1990 Jan 30;166(2):852-9. doi: 10.1016/0006-291x(90)90888-t.
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.
通过硫酸铵沉淀、DEAE-琼脂糖层析和单克隆抗体亲和层析从HL-60细胞的培养上清液中纯化出一种细胞外髓过氧化物酶前体。经十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定，纯化后的蛋白质是一种分子量约为89 kDa的糖蛋白。该蛋白质的氨基末端氨基酸序列起始于从髓过氧化物酶cDNA推导的745个氨基酸序列的第49个氨基酸残基，这表明该蛋白质由697个氨基酸残基组成。文中讨论了该前体在髓过氧化物酶加工过程中的意义。
