Studies on the cyclophorase system. XIX. Interconversion of pyridine nucleotides
The enzymatic synthesis of triphosphopyridine nucleotide (TPN) from diphosphopyridine nucleotide (DPN) and adenosine triphosphate (ATP), and the conversion of TPN to DPN has been shown in fractions derived from the cyclophorase-type particulate preparation from rabbit liver and kidney. The formation...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1951-12, Vol.34 (2), p.437-441 |
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container_title | Archives of biochemistry and biophysics |
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creator | Katchman, Bernard Betheil, Joseph J. Schepartz, Abner I. Sanadi, D.R. |
description | The enzymatic synthesis of triphosphopyridine nucleotide (TPN) from diphosphopyridine nucleotide (DPN) and adenosine triphosphate (ATP), and the conversion of TPN to DPN has been shown in fractions derived from the cyclophorase-type particulate preparation from rabbit liver and kidney. The formation of DPN from TPN occurs in the soluble fraction also. |
doi_str_mv | 10.1016/0003-9861(51)90022-7 |
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The formation of DPN from TPN occurs in the soluble fraction also.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(51)90022-7</identifier><identifier>PMID: 14904079</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Coenzymes ; Esterases ; Nucleotides ; Old Medline ; Pyridines</subject><ispartof>Archives of biochemistry and biophysics, 1951-12, Vol.34 (2), p.437-441</ispartof><rights>1951</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c275t-af83db0560537162e35e1f1fe1ed857f4e07c02fe292a90c2644ffa3b4749a4c3</citedby><cites>FETCH-LOGICAL-c275t-af83db0560537162e35e1f1fe1ed857f4e07c02fe292a90c2644ffa3b4749a4c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(51)90022-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14904079$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Katchman, Bernard</creatorcontrib><creatorcontrib>Betheil, Joseph J.</creatorcontrib><creatorcontrib>Schepartz, Abner I.</creatorcontrib><creatorcontrib>Sanadi, D.R.</creatorcontrib><title>Studies on the cyclophorase system. XIX. Interconversion of pyridine nucleotides</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The enzymatic synthesis of triphosphopyridine nucleotide (TPN) from diphosphopyridine nucleotide (DPN) and adenosine triphosphate (ATP), and the conversion of TPN to DPN has been shown in fractions derived from the cyclophorase-type particulate preparation from rabbit liver and kidney. 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subjects | Coenzymes Esterases Nucleotides Old Medline Pyridines |
title | Studies on the cyclophorase system. XIX. Interconversion of pyridine nucleotides |
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