Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.22.1 (DNase II)
 429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To provide information on the role of nucleases in oncogenic virus infection, the activities of 3'-nucleotide phosphodiesterase (3'-NPDase), 5'-nucleotide phosphodiesterase (5'-NPDase), acid deoxyribonuclease (DNase II), and 3',5'-cyclic AMP phosphodiesterase (cAMPDase) in spleen extracts of murine sarcoma virus-infected C57BL/6 inbred mice were studied. At the peak of tumor growth and of the cell-mediated cytotoxic response (CMC) against tumor-associated antigens, 3'-NPDase, 5'-NPDase, and DNase II all showed depressed activities in the spleen, whereas the activity of cAMPDase in the spleen increased at the peak of CMC and remained elevated thereafter. Serum enzyme activities of the infected mice were also determined, and only 3'-NPD-ase in serum correlated well with CMC. Inasmuch as the correlation of the tumor growth with CMC was established in this system, further study on tumors with variance between CMC and growth is necessary to determine if serum 3'-NPDase is a useful biochemical marker for CMC in vivo.
 ...
PMID:Nucleases and adenosine 3',5'-cyclic monophosphate phosphodiesterase activities in murine sarcoma virus (Moloney)-infected mice. 21 66

Phosphodiesterase I [EC 3.1.4.1] was purified from normal human urine in a highly purified state free from phosphodiesterase II, RNase, DNase I, DNase II, and phosphatase by column chromatographies of DEAE-Toyopearl, butyl-Toyopearl, Affi-Gel blue, and Sephadex G-150. The molecular weight of the enzyme was 1.9 x 10(5) and the pH optimum around 9.0 with p-nitrophenyl deoxythymidine 5'-phosphate as the substrate. The enzyme hydrolyzed the 3'-5' linkage of various dinucleoside monophosphates at approximately the same rate and the phosphodiester bonds of cyclic 3',5'-mononucleotides to produce mononucleoside 5'-phosphate. The enzyme also hydrolyzed ADP to 5'-AMP and Pi, ATP to 5'-AMP and PPi, and NAD+ to 5'-AMP and NMN. The enzyme activity was abolished by removal of metal ions with EDTA, and the metal-free enzyme was reactivated on the addition of Zn2+. The enzyme activity was also abolished by some reducing agents and the inhibition was reversed by Zn2+. The metal-free enzyme was less stable than the native enzyme, and Zn2+ and Co2+ restored the stability of the metal-free enzyme to the level of the native enzyme. The enzyme degraded oligonucleotides and high molecular nucleotides stepwise from the 3'-termini to give 5'-mononucleotides. The enzyme hydrolyzed single-stranded DNA more preferentially than double-stranded DNA. The enzyme also nicked superhelical covalently closed circular phi X174 DNA to yield first open circular DNA and then linear DNA.
 ...
PMID:Phosphodiesterase I in human urine: purification and characterization of the enzyme. 282 85

Two alkaline DNases of tentacles of actinia Radianthus macrodactylus, referred to as alk DNase I and alk DNase II, respectively, have been purified up to apparent homogeneity with consecutive column ion exchange chromatography and gel filtration. Both enzymes have a lot of common properties, such as the ability to hydrolyze very effectively p-nitrophenyl-5'-TMP and heat-denatured DNA. They both have no preferential specificity to the sugar component of the nucleic acids and effectively digest ribopolymers. Their ability to hydrolyze supercoiled DNA of the pBR322 plasmid and linear DNA of the lambda phage by "miscellaneous" exo- and endonucleolytic types of attack and to produce nucleosides, nucleotides and short oligonucleotides suggests their similarity with phosphodiesterase I (5'-exonuclease, oligonucleate 5'-nucleotidohydrolase; E.C. 3.1.4.1), isolated from rattle snake Crotalus adamenteus venom. Alk DNase II has been revealed to have some uncommon properties, such as phosphomonoesterase and hemolytic activities. The protein causes a very potent lysis of human and rabbit erythrocytes. The ability of alk DNase II to precipitate some components of normal human and rabbit blood serum as well as the inhibition of this reaction by fucose but not by another monosaccharides suggest the enzyme to have a lectin-like activity. The appearance of only one protein band during electrophoresis of alk DNase II in denaturation conditions suggests that all activities are inherent to the same molecule of protein. The possible role of alkaline DNases in the toxic effect of burning by actinia tentacles is discussed.
 ...
PMID:Some properties of alkaline DNases of tentacles of actinia Radianthus macrodactylus and their hemolytic activity. 1048 93