pubmed-article:1690146 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1690146 | lifeskim:mentions | umls-concept:C0085431 | lld:lifeskim |
pubmed-article:1690146 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:1690146 | lifeskim:mentions | umls-concept:C1956126 | lld:lifeskim |
pubmed-article:1690146 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:1690146 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:1690146 | pubmed:dateCreated | 1990-4-26 | lld:pubmed |
pubmed-article:1690146 | pubmed:abstractText | Less purified fractions of ribonuclease H IIa activity of calf thymus display divalent cation-dependent ribonuclease H activity and divalent cation-independent ribonuclease activity. Because the ratio of the two enzyme activities does not change during successive chromatographic procedures, we suggest that ribonuclease H IIa activity is indeed able to degrade both ssRNA and the RNA moiety of RNA.DNA-hybrids. Ribonuclease H IIa activity can therefore be differentiated from calf thymus ribonuclease H I and H IIb by its lack of ribonuclease H specificity. The native molecular mass of ribonuclease H IIa activity is between 23 and 28 kDa. Under denaturing conditions a 23 kDa-protein band copurifies with the enzyme activity suggesting that this enzyme is monomeric. | lld:pubmed |
pubmed-article:1690146 | pubmed:language | eng | lld:pubmed |
pubmed-article:1690146 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690146 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1690146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690146 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1690146 | pubmed:month | Mar | lld:pubmed |
pubmed-article:1690146 | pubmed:issn | 0014-4754 | lld:pubmed |
pubmed-article:1690146 | pubmed:author | pubmed-author:BüsenWW | lld:pubmed |
pubmed-article:1690146 | pubmed:author | pubmed-author:FrankPP | lld:pubmed |
pubmed-article:1690146 | pubmed:author | pubmed-author:VonwirthHH | lld:pubmed |
pubmed-article:1690146 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1690146 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1690146 | pubmed:volume | 46 | lld:pubmed |
pubmed-article:1690146 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1690146 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1690146 | pubmed:pagination | 319-21 | lld:pubmed |
pubmed-article:1690146 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
pubmed-article:1690146 | pubmed:meshHeading | pubmed-meshheading:1690146-... | lld:pubmed |
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pubmed-article:1690146 | pubmed:meshHeading | pubmed-meshheading:1690146-... | lld:pubmed |
pubmed-article:1690146 | pubmed:meshHeading | pubmed-meshheading:1690146-... | lld:pubmed |
pubmed-article:1690146 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:1690146 | pubmed:articleTitle | Calf thymus ribonuclease H IIa activity lacks ribonuclease H specificity. | lld:pubmed |
pubmed-article:1690146 | pubmed:affiliation | Lehrstuhl für Allgemeine Genetik, Universität Tübingen, Federal Republic of Germany. | lld:pubmed |
pubmed-article:1690146 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1690146 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |