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Literature summary for 3.1.22.1 extracted from

  • Ohkouchi, S.; Shibata, M.; Sasaki, M.; Koike, M.; Safig, P.; Peters, C.; Nagata, S.; Uchiyama, Y.
    Biogenesis and proteolytic processing of lysosomal DNase II (2013), PLoS ONE, 8, e59148.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome and heterophagolysosome of macrophages and mononuclear cells, two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa Mus musculus 5764
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microsome 45-kDa form of recombinant DNase II Mus musculus
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification processing of DNase II in vivo is greatly altered in the liver of mice lacking cathepsin L. DNase II is extracellularly secreted from cells overexpressing DNase II and is detected as a pro-form, which is activated under acidic conditions. In transgenic COS1 cells, a band of 45 kDa colocalizeswith ER marker protein Bip and two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa in lysosomes Mus musculus

Purification (Commentary)

Purification (Comment) Organism
partial purification using Con A Sepharose Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
bone marrow
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Mus musculus
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liver
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Mus musculus
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macrophage CD68-positive macrophage Mus musculus
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mononuclear cell
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Mus musculus
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spleen immunoreactivity is granular and localized in the red pulp Mus musculus
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