Studies on the Mechanism of Substrate Protection of Enolase and Lactic Dehydrogenase against Ionizing Radiation
Beef heart lactic dehydrogenase (LDH) and rabbit muscle enolase were used to study the protective effect of substrates against ionizing radiation. The substrate of enolase, D-glyceric acid 2-phosphate, protected enolase activity against ionizing radiation, but the protection occurred in the absence...
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| Veröffentlicht in: | Radiation research 1967-02, Vol.30 (2), p.208-216 |
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| creator | Winstead, Jack A. Gass, Arthur E. |
| description | Beef heart lactic dehydrogenase (LDH) and rabbit muscle enolase were used to study the protective effect of substrates against ionizing radiation. The substrate of enolase, D-glyceric acid 2-phosphate, protected enolase activity against ionizing radiation, but the protection occurred in the absence of magnesium ions, which are required to bind the substrate molecule to the enzyme molecule. The substrate of enolase also protected LDH. Reduced nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide (NAD) protected LDH and also enolase. In both cases NADH gave better protection. NADH was oxidized to NAD by radiation both in the presence and in the absence of protein molecules. Cytidine-2′,3′-cylic phosphate, a substrate for ribonuclease, gave partial protection to both enolase and LDH. From the results of this study, it is concluded that specific "substrate protection" is not the primary mechanism involved. The data suggest that a "radical scavenger" mechanism would best account for the observed results. |
| doi_str_mv | 10.2307/3572046 |
| format | Article |
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The substrate of enolase, D-glyceric acid 2-phosphate, protected enolase activity against ionizing radiation, but the protection occurred in the absence of magnesium ions, which are required to bind the substrate molecule to the enzyme molecule. The substrate of enolase also protected LDH. Reduced nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide (NAD) protected LDH and also enolase. In both cases NADH gave better protection. NADH was oxidized to NAD by radiation both in the presence and in the absence of protein molecules. Cytidine-2′,3′-cylic phosphate, a substrate for ribonuclease, gave partial protection to both enolase and LDH. From the results of this study, it is concluded that specific "substrate protection" is not the primary mechanism involved. The data suggest that a "radical scavenger" mechanism would best account for the observed results.</description><identifier>ISSN: 0033-7587</identifier><identifier>EISSN: 1938-5404</identifier><identifier>DOI: 10.2307/3572046</identifier><identifier>PMID: 4381270</identifier><language>eng</language><publisher>United States: Academic Press, Inc</publisher><subject>Active sites ; Carbonic Anhydrases ; Chemical Phenomena ; Chemistry ; Dehydrogenases ; Enzyme substrates ; Enzymes ; Ionizing radiation ; Irradiation ; L-Lactate Dehydrogenase ; Molecules ; NAD ; NADP ; Phosphates ; Radiation Effects ; Radiation-Protective Agents ; Salts ; Substrate specificity</subject><ispartof>Radiation research, 1967-02, Vol.30 (2), p.208-216</ispartof><rights>Copyright 1967 Academic Press Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c305t-5313ce898fbb9a735db3a4cd47eafbda81e06cb91d3dc323703e8d46c666d693</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3572046$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3572046$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4381270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Winstead, Jack A.</creatorcontrib><creatorcontrib>Gass, Arthur E.</creatorcontrib><title>Studies on the Mechanism of Substrate Protection of Enolase and Lactic Dehydrogenase against Ionizing Radiation</title><title>Radiation research</title><addtitle>Radiat Res</addtitle><description>Beef heart lactic dehydrogenase (LDH) and rabbit muscle enolase were used to study the protective effect of substrates against ionizing radiation. The substrate of enolase, D-glyceric acid 2-phosphate, protected enolase activity against ionizing radiation, but the protection occurred in the absence of magnesium ions, which are required to bind the substrate molecule to the enzyme molecule. The substrate of enolase also protected LDH. Reduced nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide (NAD) protected LDH and also enolase. In both cases NADH gave better protection. NADH was oxidized to NAD by radiation both in the presence and in the absence of protein molecules. Cytidine-2′,3′-cylic phosphate, a substrate for ribonuclease, gave partial protection to both enolase and LDH. From the results of this study, it is concluded that specific "substrate protection" is not the primary mechanism involved. The data suggest that a "radical scavenger" mechanism would best account for the observed results.</description><subject>Active sites</subject><subject>Carbonic Anhydrases</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Dehydrogenases</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Ionizing radiation</subject><subject>Irradiation</subject><subject>L-Lactate Dehydrogenase</subject><subject>Molecules</subject><subject>NAD</subject><subject>NADP</subject><subject>Phosphates</subject><subject>Radiation Effects</subject><subject>Radiation-Protective Agents</subject><subject>Salts</subject><subject>Substrate specificity</subject><issn>0033-7587</issn><issn>1938-5404</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1967</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE9PAjEUxBujQUTjJzDpwcTTartvt909GsQ_CUYj3Em3fQsl0JK2HPDTuwjx5ullZn5vDkPINWf3OTD5AKXMWSFOSJ_XUGVlwYpT0mcMIJNlJc_JRYxL1mku6h7pFVDxXLI-8ZO0NRYj9Y6mBdJ31AvlbFxT39LJtokpqIT0M_iEOtmO6vyR8ysVkSpn6Fh1tqZPuNiZ4OfofoO5si4m-uad_bZuTr-UsWr_fknOWrWKeHW8AzJ9Hk2Hr9n44-Vt-DjONLAyZSVw0FjVVds0tZJQmgZUoU0hUbWNURVHJnRTcwNGQw6SAVamEFoIYUQNA3J3qNXBxxiwnW2CXauwm3E22w82Ow7WkTcHcrNt1mj-uONCXX57yJcx-fBvzQ9K0nIM</recordid><startdate>196702</startdate><enddate>196702</enddate><creator>Winstead, Jack A.</creator><creator>Gass, Arthur E.</creator><general>Academic Press, Inc</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></search><sort><creationdate>196702</creationdate><title>Studies on the Mechanism of Substrate Protection of Enolase and Lactic Dehydrogenase against Ionizing Radiation</title><author>Winstead, Jack A. ; Gass, Arthur E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c305t-5313ce898fbb9a735db3a4cd47eafbda81e06cb91d3dc323703e8d46c666d693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1967</creationdate><topic>Active sites</topic><topic>Carbonic Anhydrases</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Dehydrogenases</topic><topic>Enzyme substrates</topic><topic>Enzymes</topic><topic>Ionizing radiation</topic><topic>Irradiation</topic><topic>L-Lactate Dehydrogenase</topic><topic>Molecules</topic><topic>NAD</topic><topic>NADP</topic><topic>Phosphates</topic><topic>Radiation Effects</topic><topic>Radiation-Protective Agents</topic><topic>Salts</topic><topic>Substrate specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Winstead, Jack A.</creatorcontrib><creatorcontrib>Gass, Arthur E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Radiation research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Winstead, Jack A.</au><au>Gass, Arthur E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on the Mechanism of Substrate Protection of Enolase and Lactic Dehydrogenase against Ionizing Radiation</atitle><jtitle>Radiation research</jtitle><addtitle>Radiat Res</addtitle><date>1967-02</date><risdate>1967</risdate><volume>30</volume><issue>2</issue><spage>208</spage><epage>216</epage><pages>208-216</pages><issn>0033-7587</issn><eissn>1938-5404</eissn><abstract>Beef heart lactic dehydrogenase (LDH) and rabbit muscle enolase were used to study the protective effect of substrates against ionizing radiation. The substrate of enolase, D-glyceric acid 2-phosphate, protected enolase activity against ionizing radiation, but the protection occurred in the absence of magnesium ions, which are required to bind the substrate molecule to the enzyme molecule. The substrate of enolase also protected LDH. Reduced nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide (NAD) protected LDH and also enolase. In both cases NADH gave better protection. NADH was oxidized to NAD by radiation both in the presence and in the absence of protein molecules. Cytidine-2′,3′-cylic phosphate, a substrate for ribonuclease, gave partial protection to both enolase and LDH. From the results of this study, it is concluded that specific "substrate protection" is not the primary mechanism involved. The data suggest that a "radical scavenger" mechanism would best account for the observed results.</abstract><cop>United States</cop><pub>Academic Press, Inc</pub><pmid>4381270</pmid><doi>10.2307/3572046</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0033-7587 |
| ispartof | Radiation research, 1967-02, Vol.30 (2), p.208-216 |
| issn | 0033-7587 1938-5404 |
| language | eng |
| recordid | cdi_crossref_primary_10_2307_3572046 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing |
| subjects | Active sites Carbonic Anhydrases Chemical Phenomena Chemistry Dehydrogenases Enzyme substrates Enzymes Ionizing radiation Irradiation L-Lactate Dehydrogenase Molecules NAD NADP Phosphates Radiation Effects Radiation-Protective Agents Salts Substrate specificity |
| title | Studies on the Mechanism of Substrate Protection of Enolase and Lactic Dehydrogenase against Ionizing Radiation |
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