Bond cleaving specificity and other properties of a deoxyribonuclease of mouse kidney

A deoxyribonuclease has been purified more than 700-fold from mouse kidney. The enzyme is mainly localized in the microsomal fraction and shows optimal activity at pH 7.8, in the presence of 1 × 10 −2 m magnesium. It is an endonuclease with preference towards the d-pN-p6 -keto base bond. The enzyme...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1969-01, Vol.135 (1), p.36-44
Hauptverfasser:	Antonoglou, O., Georgatsos, J.G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Buffers Cattle Cell Nucleus - enzymology Chemical Precipitation Chromatography, Gel Chromatography, Ion Exchange Deoxyribonucleases - antagonists & inhibitors Deoxyribonucleases - isolation & purification DNA Hydrogen-Ion Concentration Kidney - cytology Kidney - enzymology Magnesium Male Methods Mice Microsomes - enzymology Mitochondria - enzymology Nucleotides Organ Specificity Purines Pyrimidinones Quaternary Ammonium Compounds RNA Thymus Gland
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Beschreibung
Zusammenfassung:	A deoxyribonuclease has been purified more than 700-fold from mouse kidney. The enzyme is mainly localized in the microsomal fraction and shows optimal activity at pH 7.8, in the presence of 1 × 10 −2 m magnesium. It is an endonuclease with preference towards the d-pN-p6 -keto base bond. The enzyme is not active towards RNA and is inhibited by purine and pyrimidine bases, as well as by oligonucleotides of average chain length 35–40 or less.
ISSN:	0003-9861 1096-0384
DOI:	10.1016/0003-9861(69)90513-X