| pubmed-article:3214425 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3214425 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:3214425 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:3214425 | lifeskim:mentions | umls-concept:C2260821 | lld:lifeskim |
| pubmed-article:3214425 | lifeskim:mentions | umls-concept:C0635839 | lld:lifeskim |
| pubmed-article:3214425 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3214425 | pubmed:dateCreated | 1989-2-13 | lld:pubmed |
| pubmed-article:3214425 | pubmed:abstractText | The ability of bovine pancreatic DNAase to hydrolyse the synthetic substrate p-nitrophenyl phenylphosphonate (NPPP) is intrinsic and is not due to the contamination of the DNAase preparation by nonspecific phosphodiesterases because the activities of DNA and NPPP hydrolysis are co-eluted from a DEAE-cellulose column with use of the Ca2+-affinity elution method and because the two activities are decreased simultaneously when the purified enzyme is treated with Cu2+/iodoacetate, an active-site-labelling agent for DNAase. NPPP hydrolysis is facilitated by the metal ion-DNAase. At relatively high Na+ concentrations, where the metal ion-DNA interaction is weak, DNA hydrolysis is also facilitated by the metal ion-DNAase. With NPPP as substrate the Michaelis constants are Km 3.7 mM for Mn2+ and Km 49 mM for Mg2+ in 0.2 M-Tris/HCl buffer, pH 7.2. Ca2+ competes with Mn2+, with Ki 64 mM. Free Cu2+ ions non-competitively inhibit DNAase-catalysed DNA or NPPP hydrolysis in the presence of Mn2+ or Mg2+ and the inhibition is not relieved by Ca2+. The affinity of Cu2+ for free DNAase is higher than that for Mn2+-DNAase. Mn2+ is not bound to DNAase via a simple ionic interaction, as Mn2+ remains bound in the presence of relatively high Na+ concentrations and induces a near-u.v. difference absorption spectrum. The kinetics of NPPP hydrolysis catalysed by Mn2+-DNAase are sigmoidal. From the Hill equation, h = 2.0 is obtained, suggesting that more than two NPPP molecules are bound per molecule of DNAase with a certain amount of co-operativity. Because DNAase in solution is a monomer with a single catalytic site, the multiple NPPP molecules on a single protein molecule are probably in one location, resulting in a co-operative interaction that may resemble that in the stacked base-pairs of double-helical DNA. | lld:pubmed |
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| pubmed-article:3214425 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3214425 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3214425 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3214425 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3214425 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3214425 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3214425 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3214425 | pubmed:author | pubmed-author:LiaoT HTH | lld:pubmed |
| pubmed-article:3214425 | pubmed:author | pubmed-author:HsiehJ CJC | lld:pubmed |
| pubmed-article:3214425 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3214425 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3214425 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:3214425 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3214425 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3214425 | pubmed:pagination | 781-7 | lld:pubmed |
| pubmed-article:3214425 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3214425 | pubmed:meshHeading | pubmed-meshheading:3214425-... | lld:pubmed |
| pubmed-article:3214425 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3214425 | pubmed:articleTitle | Hydrolysis of p-nitrophenyl phenylphosphonate catalysed by bovine pancreatic deoxyribonuclease. | lld:pubmed |
| pubmed-article:3214425 | pubmed:affiliation | Department of Biochemistry, National Taiwan University/College of Medicine, Taipei, Republic of China. | lld:pubmed |
| pubmed-article:3214425 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3214425 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
