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• W2027660378 startingPage "15154" @default.
• W2027660378 abstract "DNase I isolated from human urine (hDNase) or expressed in Chinese hamster ovary (CHO) cells contains mannose-phosphorylated oligosaccharides. hDNase binds to a column of immobilized cation-independent mannose 6-phosphate receptor, with the strongest binding exhibited by the protein bearing diphosphorylated oligosaccharides. The binding is inhibited by 5 mM mannose 6-phosphate, and can be prevented by prior treatment of hDNase with alkaline phosphatase. Phosphorylated high-mannose oligosaccharides were observed at both sites of glycosylation in hDNase by high-performance liquid chromatography−mass spectrometry of a tryptic digest. These results indicate that hDNase, though not an acid hydrolase, may enter the lysosomal trafficking pathway, and may have evolved from a lysosomal enzyme." @default.
• W2027660378 created "2016-06-24" @default.
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• W2027660378 date "1998-10-01" @default.
• W2027660378 modified "2023-10-16" @default.
• W2027660378 title "Human DNase I Contains Mannose 6-Phosphate and Binds the Cation-Independent Mannose 6-Phosphate Receptor" @default.
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• W2027660378 doi "https://doi.org/10.1021/bi981465t" @default.
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