| pubmed-article:6056626 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6056626 | lifeskim:mentions | umls-concept:C0032548 | lld:lifeskim |
| pubmed-article:6056626 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:6056626 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:6056626 | lifeskim:mentions | umls-concept:C2348822 | lld:lifeskim |
| pubmed-article:6056626 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6056626 | pubmed:dateCreated | 1968-1-6 | lld:pubmed |
| pubmed-article:6056626 | pubmed:abstractText | 1. Treatment of Micrococcus lysodeikticus polynucleotide phosphorylase (nucleoside diphosphate-polynucleotide nucleotidyltransferase) with trypsin causes a preferential loss of its cytidine diphosphate and uridine diphosphate polymerization activities. 2. The phosphorolytic activity of the enzyme towards polycytidylic acid is unaffected in conditions in which the cytidine diphosphate-polymerization activity without added primer is virtually abolished. 3. The treated enzyme retains its altered pattern of activities when purified fivefold by gel filtration. 4. The effect on the cytidine diphosphate-polymerization activity is due, in part, to a large increase in primer requirement as a result of proteolysis, and is qualitatively independent of the state of purity of the polynucleotide phosphorylase. 5. The enzyme is protected from trypsin degradation by nucleic acids, polynucleotides and nucleoside disphosphates. 6. A similar, but less marked differential effect, is caused by alpha-chymotrypsin. | lld:pubmed |
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| pubmed-article:6056626 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6056626 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6056626 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6056626 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6056626 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6056626 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6056626 | pubmed:author | pubmed-author:FearD LDL | lld:pubmed |
| pubmed-article:6056626 | pubmed:author | pubmed-author:FittE AEA | lld:pubmed |
| pubmed-article:6056626 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6056626 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:6056626 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6056626 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6056626 | pubmed:pagination | 25-33 | lld:pubmed |
| pubmed-article:6056626 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6056626 | pubmed:meshHeading | pubmed-meshheading:6056626-... | lld:pubmed |
| pubmed-article:6056626 | pubmed:year | 1967 | lld:pubmed |
| pubmed-article:6056626 | pubmed:articleTitle | The effect of trypsin digestion on the activities of polynucleotide phosphorylase. | lld:pubmed |
| pubmed-article:6056626 | pubmed:publicationType | Journal Article | lld:pubmed |
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