pubmed-article:135758 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:135758 | lifeskim:mentions | umls-concept:C0027923 | lld:lifeskim |
pubmed-article:135758 | lifeskim:mentions | umls-concept:C2752263 | lld:lifeskim |
pubmed-article:135758 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:135758 | pubmed:dateCreated | 1976-12-30 | lld:pubmed |
pubmed-article:135758 | pubmed:abstractText | Hypoxanthine uptake and hypoxanthine phosphoribosyltransferase activity (EC 2.4.2.8) were determined in germinated conidia from the adenine auxotrophic strains ad-1 and ad-8 and the double mutant strain ad-1 ad-8. The mutant strain ad-1 appears to lack aminoimidazolecarboximide ribonucleotide formyltransferase (EC 2.1.2.3) or inosine 5'monophosphate cyclohydrolase (EC 3.5.1.10) activities, or both, whereas the ad-8 strain lacks adenylosuccinate synthase activity (EC 6.3.4.4). Normal (or wild-type) hypoxanthine transport capacity was found to the ad-1 conidia, whereas the ad-8 strains failed to take up any hypoxanthine. The double mutant strains showed intermediate transport capacities. Similar results were obtained for hypoxanthine phosphoribosyl-transferase activity assayed in germinated conidia. The ad-1 strain showed greatest activity, the ad-8 strain showed the least activity, and the double mutant strain showed intermediate activity levels. Ion-exchange chromatography of the growth media revealed that in the presence of NH+/4, the ad-8 strain excreted hypoxanthine or inosine, the ad-1 strain did not excrete any purines, and the ad-1 ad-8 double mutant strain excreted uric acid. In the absence of NH+/4, none of the strains excreted any detectable purine compounds. | lld:pubmed |
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pubmed-article:135758 | pubmed:language | eng | lld:pubmed |
pubmed-article:135758 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:135758 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:135758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:135758 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:135758 | pubmed:month | Nov | lld:pubmed |
pubmed-article:135758 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:135758 | pubmed:author | pubmed-author:MagillC WCW | lld:pubmed |
pubmed-article:135758 | pubmed:author | pubmed-author:MagillJ MJM | lld:pubmed |
pubmed-article:135758 | pubmed:author | pubmed-author:SabinaR LRL | lld:pubmed |
pubmed-article:135758 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:135758 | pubmed:volume | 128 | lld:pubmed |
pubmed-article:135758 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:135758 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:135758 | pubmed:pagination | 598-603 | lld:pubmed |
pubmed-article:135758 | pubmed:dateRevised | 2010-9-1 | lld:pubmed |
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pubmed-article:135758 | pubmed:year | 1976 | lld:pubmed |
pubmed-article:135758 | pubmed:articleTitle | Regulation of hypoxanthine transport in Neurospora crassa. | lld:pubmed |
pubmed-article:135758 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:135758 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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