Oxidation of reduced pyridine nucleotides in Pasteurella tularensis: I. Distribution of diaphorases and transhydrogenases
The particulate fraction from sonicates of P. tularensis contained a very active DPNH oxidase system, but was almost inactive with TPNH. The TPNH-DPN transhydrogenase of the cell was located in the soluble fraction, while most of the DPNH-3-acetylpyridine DPN transhydrogenase activity was in the par...
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| Veröffentlicht in: | Biochimica et biophysica acta 1961-03, Vol.48 (1), p.77-84 |
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| container_title | Biochimica et biophysica acta |
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| creator | Robinson, Diana A. Mills, R.C. |
| description | The particulate fraction from sonicates of
P. tularensis contained a very active DPNH oxidase system, but was almost inactive with TPNH. The TPNH-DPN transhydrogenase of the cell was located in the soluble fraction, while most of the DPNH-3-acetylpyridine DPN transhydrogenase activity was in the particulate fraction (or acetone powder residue). Almost no TPNH-3-acetylpyridine DPN transhydrogenase activity was present.
TPNH-DPN transhydrogenase activity could be determined by coupling with the particulate DPNH-3-acetylpyridine DPN transhydrogenase.
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of the DPNH diaphorase activity was found in the soluble fraction. The DPNH/TPNH diaphorase ratio was about 0.7 for whole sonicate, and about 0.5 for the soluble fraction. Very little TPNH diaphorase activity was observed in the particulate fraction, even after treatment with acetone, butanol, or deoxycholate, or after further sonic oscillation. |
| doi_str_mv | 10.1016/0006-3002(61)90517-0 |
| format | Article |
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P. tularensis contained a very active DPNH oxidase system, but was almost inactive with TPNH. The TPNH-DPN transhydrogenase of the cell was located in the soluble fraction, while most of the DPNH-3-acetylpyridine DPN transhydrogenase activity was in the particulate fraction (or acetone powder residue). Almost no TPNH-3-acetylpyridine DPN transhydrogenase activity was present.
TPNH-DPN transhydrogenase activity could be determined by coupling with the particulate DPNH-3-acetylpyridine DPN transhydrogenase.
About
2
3
of the DPNH diaphorase activity was found in the soluble fraction. The DPNH/TPNH diaphorase ratio was about 0.7 for whole sonicate, and about 0.5 for the soluble fraction. Very little TPNH diaphorase activity was observed in the particulate fraction, even after treatment with acetone, butanol, or deoxycholate, or after further sonic oscillation.</description><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-2434</identifier><identifier>DOI: 10.1016/0006-3002(61)90517-0</identifier><identifier>PMID: 13742274</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Dihydrolipoamide Dehydrogenase ; Francisella tularensis - metabolism ; NADP Transhydrogenases ; Nucleotides ; Old Medline ; Oxidation-Reduction ; Oxidoreductases ; Pyridines</subject><ispartof>Biochimica et biophysica acta, 1961-03, Vol.48 (1), p.77-84</ispartof><rights>1961</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13742274$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Robinson, Diana A.</creatorcontrib><creatorcontrib>Mills, R.C.</creatorcontrib><title>Oxidation of reduced pyridine nucleotides in Pasteurella tularensis: I. Distribution of diaphorases and transhydrogenases</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>The particulate fraction from sonicates of
P. tularensis contained a very active DPNH oxidase system, but was almost inactive with TPNH. The TPNH-DPN transhydrogenase of the cell was located in the soluble fraction, while most of the DPNH-3-acetylpyridine DPN transhydrogenase activity was in the particulate fraction (or acetone powder residue). Almost no TPNH-3-acetylpyridine DPN transhydrogenase activity was present.
TPNH-DPN transhydrogenase activity could be determined by coupling with the particulate DPNH-3-acetylpyridine DPN transhydrogenase.
About
2
3
of the DPNH diaphorase activity was found in the soluble fraction. The DPNH/TPNH diaphorase ratio was about 0.7 for whole sonicate, and about 0.5 for the soluble fraction. Very little TPNH diaphorase activity was observed in the particulate fraction, even after treatment with acetone, butanol, or deoxycholate, or after further sonic oscillation.</description><subject>Dihydrolipoamide Dehydrogenase</subject><subject>Francisella tularensis - metabolism</subject><subject>NADP Transhydrogenases</subject><subject>Nucleotides</subject><subject>Old Medline</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>Pyridines</subject><issn>0006-3002</issn><issn>1878-2434</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1961</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kUtLxDAQgIMouj7-gUhOoodqpmmbxoMg6xMEPeg5pM1EI910TVJx_72tr9MMwzfDzDeE7AM7AQbVKWOsyjhj-VEFx5KVIDK2RmZQizrLC16sk9k_skW2Y3wbk5IzuUm2gIsiz0UxI6uHT2d0cr2nvaUBzdCioctVcMZ5pH5oO-yTMxip8_RRx4RDwK7TNA2dDuiji2f07oReupiCa4a_Ucbp5WsfdBw7tTc0Be3j68qE_gX9VN0lG1Z3Efd-4w55vr56mt9m9w83d_OL-wxByJQVkrfMNrKyJYOyFGAkVrVAyY0cNaDNgbfQ2LJsmCxAIOfWMgsCdM5tg3yHHP7MXYb-fcCY1MLFdjrBYz9EVeei5lKWI3jwCw7NAo1aBrfQYaX-ZI3A-Q-A47ofDoOKrUM_CnMB26RM7xQwNX1HTerVpF5VoL6_oxj_AlK1gm0</recordid><startdate>19610318</startdate><enddate>19610318</enddate><creator>Robinson, Diana A.</creator><creator>Mills, R.C.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19610318</creationdate><title>Oxidation of reduced pyridine nucleotides in Pasteurella tularensis: I. Distribution of diaphorases and transhydrogenases</title><author>Robinson, Diana A. ; Mills, R.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e179t-493c0fb96f5015571d9e687e93d9016ef213c1bf55b09417e33ff0f171a23fbe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1961</creationdate><topic>Dihydrolipoamide Dehydrogenase</topic><topic>Francisella tularensis - metabolism</topic><topic>NADP Transhydrogenases</topic><topic>Nucleotides</topic><topic>Old Medline</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases</topic><topic>Pyridines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Robinson, Diana A.</creatorcontrib><creatorcontrib>Mills, R.C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robinson, Diana A.</au><au>Mills, R.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxidation of reduced pyridine nucleotides in Pasteurella tularensis: I. Distribution of diaphorases and transhydrogenases</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>1961-03-18</date><risdate>1961</risdate><volume>48</volume><issue>1</issue><spage>77</spage><epage>84</epage><pages>77-84</pages><issn>0006-3002</issn><eissn>1878-2434</eissn><abstract>The particulate fraction from sonicates of
P. tularensis contained a very active DPNH oxidase system, but was almost inactive with TPNH. The TPNH-DPN transhydrogenase of the cell was located in the soluble fraction, while most of the DPNH-3-acetylpyridine DPN transhydrogenase activity was in the particulate fraction (or acetone powder residue). Almost no TPNH-3-acetylpyridine DPN transhydrogenase activity was present.
TPNH-DPN transhydrogenase activity could be determined by coupling with the particulate DPNH-3-acetylpyridine DPN transhydrogenase.
About
2
3
of the DPNH diaphorase activity was found in the soluble fraction. The DPNH/TPNH diaphorase ratio was about 0.7 for whole sonicate, and about 0.5 for the soluble fraction. Very little TPNH diaphorase activity was observed in the particulate fraction, even after treatment with acetone, butanol, or deoxycholate, or after further sonic oscillation.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>13742274</pmid><doi>10.1016/0006-3002(61)90517-0</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biochimica et biophysica acta, 1961-03, Vol.48 (1), p.77-84 |
| issn | 0006-3002 1878-2434 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Dihydrolipoamide Dehydrogenase Francisella tularensis - metabolism NADP Transhydrogenases Nucleotides Old Medline Oxidation-Reduction Oxidoreductases Pyridines |
| title | Oxidation of reduced pyridine nucleotides in Pasteurella tularensis: I. Distribution of diaphorases and transhydrogenases |
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