Purification of a lysosomal DNase from Drosophila melanogaster.
An acid DNase was purified from Drosophila melanogaster till apparent homogeneity by six consecutive chromatographic steps. The enzyme is a lysosomal DNase, because it is glycosylated and carries 1.8-2.4 mol of mannose-6-phosphate/mol of enzyme. The enzyme is fully active without any divalent cation and introduces single stranded nicks into a supercoiled DNA.
Gaszner
M
M
Institute of Biochemistry, Hungarian Academy of Sciences, Szeged.
Udvardy
A
A
D000818:Animals; D002845:Chromatography; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000196:embryology / Q000201:enzymology*; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D004625:Embryo, Nonmammalian / Q000201:enzymology; D006882:Hydroxyapatites; D007700:Kinetics; D008247:Lysosomes / Q000201:enzymology*; D010957:Plasmids
D006882:Hydroxyapatites; D017886:Durapatite; D003851:Deoxyribonucleases