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Oxidation of Reduced Triphosphopyridine Nucleotide by Guinea Pig Polymorphonuclear Leucocytes
THE phagocytic process in guinea pig polymorphonuclear leucocytes (PMN) is accompanied by increases in the rates of oxygen consumption, of glucose oxidation by the hexosemonophosphate shunt and of formate oxidation to carbon dioxide 1–3 . The availability of triphosphopyridine nucleotido (NADP) appe...
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| Published in: | Nature (London) 1964-04, Vol.202 (4927), p.85-86 |
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| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c315t-55d7752a1c064df095f4007262549589995993f9947f96e9279e905ecd21dd3c3 |
| container_end_page | 86 |
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| container_title | Nature (London) |
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| creator | ROBERTS, J. QUASTEL, J. H. |
| description | THE phagocytic process in guinea pig polymorphonuclear leucocytes (PMN) is accompanied by increases in the rates of oxygen consumption, of glucose oxidation by the hexosemonophosphate shunt and of formate oxidation to carbon dioxide
1–3
. The availability of triphosphopyridine nucleotido (NADP) appears to regulate the rate of glucose oxidation by the shunt in leucocytes
3,4
. Attempts have been made to correlate the stimulated activity of the hexosemonophosphate shunt in phagocytizing leucocytes with increased NADPH oxidation. The evidence indicates that NADPH oxidation in phagocytizing leucocytes is not accomplished by the classical route of hydrogen transport by way of cytochrome reductase and cytochrome
c
(ref. 1) nor by means of an NADP-linked lactate dehydrogenase
2
. Iyer, Islam and Quastal
2,3
obtained results showing that PMN possess an enzyme system capable of oxidizing NADPH and NADH by a reaction involving the formation of hydrogen peroxide. The enzyme, however, is much more active towards NADPH than towards NADH and its activity is strongly enhanced by manganese ions
3
. Rechcigl and Evans
5
have suggested that a hydrogen-peroxide-destroying system, such as myeloperoxidase, which is found in high concentrations in leucocytes
6
may be important in protecting the cell from toxic effects of hydrogen peroxide. Results described here show that the oxidation of reduced triphosphopyridine nucleotide in PMN may be accomplished by a reaction involving peroxidase. |
| doi_str_mv | 10.1038/202085a0 |
| format | article |
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1–3
. The availability of triphosphopyridine nucleotido (NADP) appears to regulate the rate of glucose oxidation by the shunt in leucocytes
3,4
. Attempts have been made to correlate the stimulated activity of the hexosemonophosphate shunt in phagocytizing leucocytes with increased NADPH oxidation. The evidence indicates that NADPH oxidation in phagocytizing leucocytes is not accomplished by the classical route of hydrogen transport by way of cytochrome reductase and cytochrome
c
(ref. 1) nor by means of an NADP-linked lactate dehydrogenase
2
. Iyer, Islam and Quastal
2,3
obtained results showing that PMN possess an enzyme system capable of oxidizing NADPH and NADH by a reaction involving the formation of hydrogen peroxide. The enzyme, however, is much more active towards NADPH than towards NADH and its activity is strongly enhanced by manganese ions
3
. Rechcigl and Evans
5
have suggested that a hydrogen-peroxide-destroying system, such as myeloperoxidase, which is found in high concentrations in leucocytes
6
may be important in protecting the cell from toxic effects of hydrogen peroxide. Results described here show that the oxidation of reduced triphosphopyridine nucleotide in PMN may be accomplished by a reaction involving peroxidase.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/202085a0</identifier><identifier>PMID: 14166725</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Catalase ; Cyanides ; Formates ; Guinea Pigs ; Humanities and Social Sciences ; Hydrogen Peroxide ; letter ; Leukocytes ; Manganese ; Manometry ; multidisciplinary ; NADP ; Neutrophils ; Old Medline ; Oxidation-Reduction ; Peroxidases ; Phagocytosis ; Pharmacology ; Science ; Science (multidisciplinary) ; Spectrophotometry</subject><ispartof>Nature (London), 1964-04, Vol.202 (4927), p.85-86</ispartof><rights>Springer Nature Limited 1964</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c315t-55d7752a1c064df095f4007262549589995993f9947f96e9279e905ecd21dd3c3</citedby><cites>FETCH-LOGICAL-c315t-55d7752a1c064df095f4007262549589995993f9947f96e9279e905ecd21dd3c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14166725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ROBERTS, J.</creatorcontrib><creatorcontrib>QUASTEL, J. H.</creatorcontrib><title>Oxidation of Reduced Triphosphopyridine Nucleotide by Guinea Pig Polymorphonuclear Leucocytes</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>THE phagocytic process in guinea pig polymorphonuclear leucocytes (PMN) is accompanied by increases in the rates of oxygen consumption, of glucose oxidation by the hexosemonophosphate shunt and of formate oxidation to carbon dioxide
1–3
. The availability of triphosphopyridine nucleotido (NADP) appears to regulate the rate of glucose oxidation by the shunt in leucocytes
3,4
. Attempts have been made to correlate the stimulated activity of the hexosemonophosphate shunt in phagocytizing leucocytes with increased NADPH oxidation. The evidence indicates that NADPH oxidation in phagocytizing leucocytes is not accomplished by the classical route of hydrogen transport by way of cytochrome reductase and cytochrome
c
(ref. 1) nor by means of an NADP-linked lactate dehydrogenase
2
. Iyer, Islam and Quastal
2,3
obtained results showing that PMN possess an enzyme system capable of oxidizing NADPH and NADH by a reaction involving the formation of hydrogen peroxide. The enzyme, however, is much more active towards NADPH than towards NADH and its activity is strongly enhanced by manganese ions
3
. Rechcigl and Evans
5
have suggested that a hydrogen-peroxide-destroying system, such as myeloperoxidase, which is found in high concentrations in leucocytes
6
may be important in protecting the cell from toxic effects of hydrogen peroxide. Results described here show that the oxidation of reduced triphosphopyridine nucleotide in PMN may be accomplished by a reaction involving peroxidase.</description><subject>Animals</subject><subject>Catalase</subject><subject>Cyanides</subject><subject>Formates</subject><subject>Guinea Pigs</subject><subject>Humanities and Social Sciences</subject><subject>Hydrogen Peroxide</subject><subject>letter</subject><subject>Leukocytes</subject><subject>Manganese</subject><subject>Manometry</subject><subject>multidisciplinary</subject><subject>NADP</subject><subject>Neutrophils</subject><subject>Old Medline</subject><subject>Oxidation-Reduction</subject><subject>Peroxidases</subject><subject>Phagocytosis</subject><subject>Pharmacology</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Spectrophotometry</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1964</creationdate><recordtype>article</recordtype><recordid>eNpl0F1LwzAUBuAgis4P8BdIrkQvqidp0jSXMvyC4YbMSyldcjojXTOTFuy_t2MTL7wIB3IeXjgvIecMbhik-S0HDrksYY-MmFBZIrJc7ZMRAM8TyNPsiBzH-AkAkilxSI6YYFmmuByR9-m3s2XrfEN9RV_RdgYtnQe3_vBxeOs-OOsapC-dqdG3ziJd9PSxG_5KOnNLOvN1v_JhsM2GlIFOsDPe9C3GU3JQlXXEs908IW8P9_PxUzKZPj6P7yaJSZlsEymtUpKXzEAmbAVaVgJA8YxLoWWutZZap5XWQlU6Q82VRg0SjeXM2tSkJ-Rym7sO_qvD2BYrFw3Wddmg72KRp5JrIdIBXm2hCT7GgFWxDm5Vhr5gUGyqLH6rHOjFLrNbrND-wV13A7jegjismiWG4tN3oRnu_B_2A24yeyk</recordid><startdate>19640404</startdate><enddate>19640404</enddate><creator>ROBERTS, J.</creator><creator>QUASTEL, J. H.</creator><general>Nature Publishing Group UK</general><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>7X8</scope></search><sort><creationdate>19640404</creationdate><title>Oxidation of Reduced Triphosphopyridine Nucleotide by Guinea Pig Polymorphonuclear Leucocytes</title><author>ROBERTS, J. ; QUASTEL, J. H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-55d7752a1c064df095f4007262549589995993f9947f96e9279e905ecd21dd3c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1964</creationdate><topic>Animals</topic><topic>Catalase</topic><topic>Cyanides</topic><topic>Formates</topic><topic>Guinea Pigs</topic><topic>Humanities and Social Sciences</topic><topic>Hydrogen Peroxide</topic><topic>letter</topic><topic>Leukocytes</topic><topic>Manganese</topic><topic>Manometry</topic><topic>multidisciplinary</topic><topic>NADP</topic><topic>Neutrophils</topic><topic>Old Medline</topic><topic>Oxidation-Reduction</topic><topic>Peroxidases</topic><topic>Phagocytosis</topic><topic>Pharmacology</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ROBERTS, J.</creatorcontrib><creatorcontrib>QUASTEL, J. H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ROBERTS, J.</au><au>QUASTEL, J. H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxidation of Reduced Triphosphopyridine Nucleotide by Guinea Pig Polymorphonuclear Leucocytes</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1964-04-04</date><risdate>1964</risdate><volume>202</volume><issue>4927</issue><spage>85</spage><epage>86</epage><pages>85-86</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>THE phagocytic process in guinea pig polymorphonuclear leucocytes (PMN) is accompanied by increases in the rates of oxygen consumption, of glucose oxidation by the hexosemonophosphate shunt and of formate oxidation to carbon dioxide
1–3
. The availability of triphosphopyridine nucleotido (NADP) appears to regulate the rate of glucose oxidation by the shunt in leucocytes
3,4
. Attempts have been made to correlate the stimulated activity of the hexosemonophosphate shunt in phagocytizing leucocytes with increased NADPH oxidation. The evidence indicates that NADPH oxidation in phagocytizing leucocytes is not accomplished by the classical route of hydrogen transport by way of cytochrome reductase and cytochrome
c
(ref. 1) nor by means of an NADP-linked lactate dehydrogenase
2
. Iyer, Islam and Quastal
2,3
obtained results showing that PMN possess an enzyme system capable of oxidizing NADPH and NADH by a reaction involving the formation of hydrogen peroxide. The enzyme, however, is much more active towards NADPH than towards NADH and its activity is strongly enhanced by manganese ions
3
. Rechcigl and Evans
5
have suggested that a hydrogen-peroxide-destroying system, such as myeloperoxidase, which is found in high concentrations in leucocytes
6
may be important in protecting the cell from toxic effects of hydrogen peroxide. Results described here show that the oxidation of reduced triphosphopyridine nucleotide in PMN may be accomplished by a reaction involving peroxidase.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>14166725</pmid><doi>10.1038/202085a0</doi><tpages>2</tpages></addata></record> |
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| ispartof | Nature (London), 1964-04, Vol.202 (4927), p.85-86 |
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| source | Springer Nature - Connect here FIRST to enable access |
| subjects | Animals Catalase Cyanides Formates Guinea Pigs Humanities and Social Sciences Hydrogen Peroxide letter Leukocytes Manganese Manometry multidisciplinary NADP Neutrophils Old Medline Oxidation-Reduction Peroxidases Phagocytosis Pharmacology Science Science (multidisciplinary) Spectrophotometry |
| title | Oxidation of Reduced Triphosphopyridine Nucleotide by Guinea Pig Polymorphonuclear Leucocytes |
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