Stimulation of human erythrocyte 2,3-bisphosphoglycerate phosphatase by vanadate
The rates of vanadate-stimulated hydrolysis of 2,3-bisphosphoglycerate in metabolically competent erythrocytes and in hemolysates were determined from data on time courses up to 35 min employing 31P nuclear magnetic resonance spectroscopy. The enhanced rate of hydrolysis of the bisphosphate was attr...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1990, Vol.276 (1), p.160-171 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Mendz, George L. Hyslop, Serena J. Kuchel, Philip W. |
| description | The rates of vanadate-stimulated hydrolysis of 2,3-bisphosphoglycerate in metabolically competent erythrocytes and in hemolysates were determined from data on time courses up to 35 min employing
31P nuclear magnetic resonance spectroscopy. The enhanced rate of hydrolysis of the bisphosphate was attributed principally to the activation of the phosphatase activity of 2,3-bisphosphoglycerate synthase both in cell suspensions and in hemolysates. Information on the concentrations of vanadate and vanadyl present in the preparations was obtained employing
51V nuclear magnetic resonance spectroscopy and electron paramagnetic resonance spectroscopy. Redox reactions involving vanadium ions appeared to be important in establishing the final equilibrium concentrations of the oxy- and oxoions (vanadate and vanadyl, respectively), but the data suggested that the activation of the enzyme resulted from direct action of the vanadium ions on the enzyme and not as a consequence of the alteration in the equilibrium of intracellular oxidants and reductants. |
| doi_str_mv | 10.1016/0003-9861(90)90023-R |
| format | Article |
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31P nuclear magnetic resonance spectroscopy. The enhanced rate of hydrolysis of the bisphosphate was attributed principally to the activation of the phosphatase activity of 2,3-bisphosphoglycerate synthase both in cell suspensions and in hemolysates. Information on the concentrations of vanadate and vanadyl present in the preparations was obtained employing
51V nuclear magnetic resonance spectroscopy and electron paramagnetic resonance spectroscopy. Redox reactions involving vanadium ions appeared to be important in establishing the final equilibrium concentrations of the oxy- and oxoions (vanadate and vanadyl, respectively), but the data suggested that the activation of the enzyme resulted from direct action of the vanadium ions on the enzyme and not as a consequence of the alteration in the equilibrium of intracellular oxidants and reductants.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(90)90023-R</identifier><identifier>PMID: 2153361</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Biological Transport ; Electron Spin Resonance Spectroscopy ; Enzymes and enzyme inhibitors ; erythrocytes ; Erythrocytes - enzymology ; Fundamental and applied biological sciences. Psychology ; Glutathione - pharmacology ; Humans ; Hydrolases ; In Vitro Techniques ; Kinetics ; Magnetic Resonance Spectroscopy ; man ; NAD - pharmacology ; Phosphoric Monoester Hydrolases - blood ; vanadate ; Vanadates - blood ; Vanadates - pharmacology</subject><ispartof>Archives of biochemistry and biophysics, 1990, Vol.276 (1), p.160-171</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-7c3a89463e52ad43f07107bd086aacc1475f77263bfa0661ee70d592e86df7f63</citedby><cites>FETCH-LOGICAL-c418t-7c3a89463e52ad43f07107bd086aacc1475f77263bfa0661ee70d592e86df7f63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/000398619090023R$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19521779$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2153361$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mendz, George L.</creatorcontrib><creatorcontrib>Hyslop, Serena J.</creatorcontrib><creatorcontrib>Kuchel, Philip W.</creatorcontrib><title>Stimulation of human erythrocyte 2,3-bisphosphoglycerate phosphatase by vanadate</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The rates of vanadate-stimulated hydrolysis of 2,3-bisphosphoglycerate in metabolically competent erythrocytes and in hemolysates were determined from data on time courses up to 35 min employing
31P nuclear magnetic resonance spectroscopy. The enhanced rate of hydrolysis of the bisphosphate was attributed principally to the activation of the phosphatase activity of 2,3-bisphosphoglycerate synthase both in cell suspensions and in hemolysates. Information on the concentrations of vanadate and vanadyl present in the preparations was obtained employing
51V nuclear magnetic resonance spectroscopy and electron paramagnetic resonance spectroscopy. Redox reactions involving vanadium ions appeared to be important in establishing the final equilibrium concentrations of the oxy- and oxoions (vanadate and vanadyl, respectively), but the data suggested that the activation of the enzyme resulted from direct action of the vanadium ions on the enzyme and not as a consequence of the alteration in the equilibrium of intracellular oxidants and reductants.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Enzymes and enzyme inhibitors</subject><subject>erythrocytes</subject><subject>Erythrocytes - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutathione - pharmacology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>man</subject><subject>NAD - pharmacology</subject><subject>Phosphoric Monoester Hydrolases - blood</subject><subject>vanadate</subject><subject>Vanadates - blood</subject><subject>Vanadates - pharmacology</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF2L1TAQhoMo69nVf6DQG0XB6iRpkuZGkGX9gAVl1eswTSeeSD-OSbvQf2_rOax3ehEC7zzzJjyMPeHwmgPXbwBAlrbW_IWFlxZAyPLmHttxsLoEWVf32e4OecjOc_4JwHmlxRk7E1xJqfmOffk6xX7ucIrjUIyh2M89DgWlZdqn0S8TFeKVLJuYD_txOz-6xVPCNT8GOGGmolmKWxywXfNH7EHALtPj033Bvr-_-nb5sbz-_OHT5bvr0le8nkrjJda20pKUwLaSAQwH07RQa0TveWVUMEZo2QQErTmRgVZZQbVugwlaXrDnx95DGn_NlCfXx-yp63Cgcc7OWGVB2P-DXFXKSGVXsDqCPo05JwrukGKPaXEc3GbcbTrdptNZcH-Mu5t17empf256au-WTorX-bPTHLPHLiQcfMx_u60S3Jjt-bdHjlZrt5GSyz7S4KmNifzk2jH--yO_AUeGnNY</recordid><startdate>1990</startdate><enddate>1990</enddate><creator>Mendz, George L.</creator><creator>Hyslop, Serena J.</creator><creator>Kuchel, Philip W.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1990</creationdate><title>Stimulation of human erythrocyte 2,3-bisphosphoglycerate phosphatase by vanadate</title><author>Mendz, George L. ; Hyslop, Serena J. ; Kuchel, Philip W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-7c3a89463e52ad43f07107bd086aacc1475f77263bfa0661ee70d592e86df7f63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Enzymes and enzyme inhibitors</topic><topic>erythrocytes</topic><topic>Erythrocytes - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutathione - pharmacology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>man</topic><topic>NAD - pharmacology</topic><topic>Phosphoric Monoester Hydrolases - blood</topic><topic>vanadate</topic><topic>Vanadates - blood</topic><topic>Vanadates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mendz, George L.</creatorcontrib><creatorcontrib>Hyslop, Serena J.</creatorcontrib><creatorcontrib>Kuchel, Philip W.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mendz, George L.</au><au>Hyslop, Serena J.</au><au>Kuchel, Philip W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stimulation of human erythrocyte 2,3-bisphosphoglycerate phosphatase by vanadate</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1990</date><risdate>1990</risdate><volume>276</volume><issue>1</issue><spage>160</spage><epage>171</epage><pages>160-171</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The rates of vanadate-stimulated hydrolysis of 2,3-bisphosphoglycerate in metabolically competent erythrocytes and in hemolysates were determined from data on time courses up to 35 min employing
31P nuclear magnetic resonance spectroscopy. The enhanced rate of hydrolysis of the bisphosphate was attributed principally to the activation of the phosphatase activity of 2,3-bisphosphoglycerate synthase both in cell suspensions and in hemolysates. Information on the concentrations of vanadate and vanadyl present in the preparations was obtained employing
51V nuclear magnetic resonance spectroscopy and electron paramagnetic resonance spectroscopy. Redox reactions involving vanadium ions appeared to be important in establishing the final equilibrium concentrations of the oxy- and oxoions (vanadate and vanadyl, respectively), but the data suggested that the activation of the enzyme resulted from direct action of the vanadium ions on the enzyme and not as a consequence of the alteration in the equilibrium of intracellular oxidants and reductants.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2153361</pmid><doi>10.1016/0003-9861(90)90023-R</doi><tpages>12</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1990, Vol.276 (1), p.160-171 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Biological Transport Electron Spin Resonance Spectroscopy Enzymes and enzyme inhibitors erythrocytes Erythrocytes - enzymology Fundamental and applied biological sciences. Psychology Glutathione - pharmacology Humans Hydrolases In Vitro Techniques Kinetics Magnetic Resonance Spectroscopy man NAD - pharmacology Phosphoric Monoester Hydrolases - blood vanadate Vanadates - blood Vanadates - pharmacology |
| title | Stimulation of human erythrocyte 2,3-bisphosphoglycerate phosphatase by vanadate |
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