Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures
1. 1. The effect of Cd 2+ on the ATPase activity of microsomal membrane preparations of Anodonta gills was studied at assay temperatures from 4°C to 39°C. 2. 2. The ATPase activity was relatively nonspecific towards divalent cations at 39°C: Cd 2+ as well as Mg 2+ and Ca 2+ activated ATPase with V m...
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| Veröffentlicht in: | Journal of thermal biology 1996, Vol.21 (2), p.77-84 |
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| container_title | Journal of thermal biology |
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| creator | Pivovarova, N.B. Lagerspetz, K.Y.H. |
| description | 1.
1. The effect of Cd
2+ on the ATPase activity of microsomal membrane preparations of
Anodonta gills was studied at assay temperatures from 4°C to 39°C.
2.
2. The ATPase activity was relatively nonspecific towards divalent cations at 39°C: Cd
2+ as well as Mg
2+ and Ca
2+ activated ATPase with
V
max being, respectively, 25.7, 33.6 and 34.8 μmol Pi·mg
−1 protein·h
−1.
3.
3. Apparent
K
a was highest for Ca
2+ and lowest for Cd
2+ at all temperatures studied. A decrease in temperature caused a fall in
V
max for all three cations, while there was no effect on the apparent
K
a for Mg
2+ but a significant decrease in apparent
K
a for Cd
2+ (from 0.4 to 0.14 mM).
4.
4. At all temperatures studied Cd
2+, but not Ca
2+, could replace Mg
2+ as the cofactor for activation of the ouabain-insensitive (Na
+ or K
+)-ATPase.
5.
5. Cd
2+ caused an inhibitory effect on ATPase in the presence of other divalent cations, Mg
2+-ATPase being more sensitive to Cd
2+ than Ca
2+-ATPase. The inhibition of Mg
2+-ATPase was competitive at 10°C and 4°C but not at higher temperatures.
6.
6. Some of the toxic effects of Cd
2+ on the
Anodonta gill ATPase at ecological temperatures are probably due to competition for Mg
2+ binding sites. |
| doi_str_mv | 10.1016/0306-4565(95)00025-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_15655107</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0306456595000259</els_id><sourcerecordid>15655107</sourcerecordid><originalsourceid>FETCH-LOGICAL-c335t-d63f6a7fb6067b34cbc12dd2b60c99ffe353aaf8bec96d92088b266ed04471763</originalsourceid><addsrcrecordid>eNp9kEtLAzEUhYMoWKv_wEVWoovRZDLJTDZCkfqAgi7qOmSSOzUyj5qkhfn3Zqy4dHW58J0D50PokpJbSqi4I4yIrOCCX0t-QwjJeSaP0IxWpcyIlPkxmv0hp-gshE9CKGeczJBdNg2YiIcGG207t-vw0OP4AXixftMBsDbR7V0csevxxrVtmNBFP9ihjxqbcdODxjpi61KRhz5iHYIecYRuC17HnYdwjk4a3Qa4-L1z9P64XD88Z6vXp5eHxSozjPGYWcEaocumFkSUNStMbWhubZ5-I2WqZ5xp3VQ1GCmszElV1bkQYElRlLQUbI6uDr1bP3ztIETVuWCgbXUPwy4omvZzSsoEFgfQ-CEED43aetdpPypK1KRUTb7U5EtJrn6UKpli94cYpBF7B14F46A3YJ1PEpUd3P8F39c8fjQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15655107</pqid></control><display><type>article</type><title>Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures</title><source>Elsevier ScienceDirect Journals</source><creator>Pivovarova, N.B. ; Lagerspetz, K.Y.H.</creator><creatorcontrib>Pivovarova, N.B. ; Lagerspetz, K.Y.H.</creatorcontrib><description>1.
1. The effect of Cd
2+ on the ATPase activity of microsomal membrane preparations of
Anodonta gills was studied at assay temperatures from 4°C to 39°C.
2.
2. The ATPase activity was relatively nonspecific towards divalent cations at 39°C: Cd
2+ as well as Mg
2+ and Ca
2+ activated ATPase with
V
max being, respectively, 25.7, 33.6 and 34.8 μmol Pi·mg
−1 protein·h
−1.
3.
3. Apparent
K
a was highest for Ca
2+ and lowest for Cd
2+ at all temperatures studied. A decrease in temperature caused a fall in
V
max for all three cations, while there was no effect on the apparent
K
a for Mg
2+ but a significant decrease in apparent
K
a for Cd
2+ (from 0.4 to 0.14 mM).
4.
4. At all temperatures studied Cd
2+, but not Ca
2+, could replace Mg
2+ as the cofactor for activation of the ouabain-insensitive (Na
+ or K
+)-ATPase.
5.
5. Cd
2+ caused an inhibitory effect on ATPase in the presence of other divalent cations, Mg
2+-ATPase being more sensitive to Cd
2+ than Ca
2+-ATPase. The inhibition of Mg
2+-ATPase was competitive at 10°C and 4°C but not at higher temperatures.
6.
6. Some of the toxic effects of Cd
2+ on the
Anodonta gill ATPase at ecological temperatures are probably due to competition for Mg
2+ binding sites.</description><identifier>ISSN: 0306-4565</identifier><identifier>EISSN: 1879-0992</identifier><identifier>DOI: 10.1016/0306-4565(95)00025-9</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Anodonta cygnea ; ATPases ; cadmium ; Freshwater ; gills ; molluscs ; temperature</subject><ispartof>Journal of thermal biology, 1996, Vol.21 (2), p.77-84</ispartof><rights>1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-d63f6a7fb6067b34cbc12dd2b60c99ffe353aaf8bec96d92088b266ed04471763</citedby><cites>FETCH-LOGICAL-c335t-d63f6a7fb6067b34cbc12dd2b60c99ffe353aaf8bec96d92088b266ed04471763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0306456595000259$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Pivovarova, N.B.</creatorcontrib><creatorcontrib>Lagerspetz, K.Y.H.</creatorcontrib><title>Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures</title><title>Journal of thermal biology</title><description>1.
1. The effect of Cd
2+ on the ATPase activity of microsomal membrane preparations of
Anodonta gills was studied at assay temperatures from 4°C to 39°C.
2.
2. The ATPase activity was relatively nonspecific towards divalent cations at 39°C: Cd
2+ as well as Mg
2+ and Ca
2+ activated ATPase with
V
max being, respectively, 25.7, 33.6 and 34.8 μmol Pi·mg
−1 protein·h
−1.
3.
3. Apparent
K
a was highest for Ca
2+ and lowest for Cd
2+ at all temperatures studied. A decrease in temperature caused a fall in
V
max for all three cations, while there was no effect on the apparent
K
a for Mg
2+ but a significant decrease in apparent
K
a for Cd
2+ (from 0.4 to 0.14 mM).
4.
4. At all temperatures studied Cd
2+, but not Ca
2+, could replace Mg
2+ as the cofactor for activation of the ouabain-insensitive (Na
+ or K
+)-ATPase.
5.
5. Cd
2+ caused an inhibitory effect on ATPase in the presence of other divalent cations, Mg
2+-ATPase being more sensitive to Cd
2+ than Ca
2+-ATPase. The inhibition of Mg
2+-ATPase was competitive at 10°C and 4°C but not at higher temperatures.
6.
6. Some of the toxic effects of Cd
2+ on the
Anodonta gill ATPase at ecological temperatures are probably due to competition for Mg
2+ binding sites.</description><subject>Anodonta cygnea</subject><subject>ATPases</subject><subject>cadmium</subject><subject>Freshwater</subject><subject>gills</subject><subject>molluscs</subject><subject>temperature</subject><issn>0306-4565</issn><issn>1879-0992</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNp9kEtLAzEUhYMoWKv_wEVWoovRZDLJTDZCkfqAgi7qOmSSOzUyj5qkhfn3Zqy4dHW58J0D50PokpJbSqi4I4yIrOCCX0t-QwjJeSaP0IxWpcyIlPkxmv0hp-gshE9CKGeczJBdNg2YiIcGG207t-vw0OP4AXixftMBsDbR7V0csevxxrVtmNBFP9ihjxqbcdODxjpi61KRhz5iHYIecYRuC17HnYdwjk4a3Qa4-L1z9P64XD88Z6vXp5eHxSozjPGYWcEaocumFkSUNStMbWhubZ5-I2WqZ5xp3VQ1GCmszElV1bkQYElRlLQUbI6uDr1bP3ztIETVuWCgbXUPwy4omvZzSsoEFgfQ-CEED43aetdpPypK1KRUTb7U5EtJrn6UKpli94cYpBF7B14F46A3YJ1PEpUd3P8F39c8fjQ</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Pivovarova, N.B.</creator><creator>Lagerspetz, K.Y.H.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope></search><sort><creationdate>1996</creationdate><title>Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures</title><author>Pivovarova, N.B. ; Lagerspetz, K.Y.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-d63f6a7fb6067b34cbc12dd2b60c99ffe353aaf8bec96d92088b266ed04471763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Anodonta cygnea</topic><topic>ATPases</topic><topic>cadmium</topic><topic>Freshwater</topic><topic>gills</topic><topic>molluscs</topic><topic>temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pivovarova, N.B.</creatorcontrib><creatorcontrib>Lagerspetz, K.Y.H.</creatorcontrib><collection>CrossRef</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Journal of thermal biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pivovarova, N.B.</au><au>Lagerspetz, K.Y.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures</atitle><jtitle>Journal of thermal biology</jtitle><date>1996</date><risdate>1996</risdate><volume>21</volume><issue>2</issue><spage>77</spage><epage>84</epage><pages>77-84</pages><issn>0306-4565</issn><eissn>1879-0992</eissn><abstract>1.
1. The effect of Cd
2+ on the ATPase activity of microsomal membrane preparations of
Anodonta gills was studied at assay temperatures from 4°C to 39°C.
2.
2. The ATPase activity was relatively nonspecific towards divalent cations at 39°C: Cd
2+ as well as Mg
2+ and Ca
2+ activated ATPase with
V
max being, respectively, 25.7, 33.6 and 34.8 μmol Pi·mg
−1 protein·h
−1.
3.
3. Apparent
K
a was highest for Ca
2+ and lowest for Cd
2+ at all temperatures studied. A decrease in temperature caused a fall in
V
max for all three cations, while there was no effect on the apparent
K
a for Mg
2+ but a significant decrease in apparent
K
a for Cd
2+ (from 0.4 to 0.14 mM).
4.
4. At all temperatures studied Cd
2+, but not Ca
2+, could replace Mg
2+ as the cofactor for activation of the ouabain-insensitive (Na
+ or K
+)-ATPase.
5.
5. Cd
2+ caused an inhibitory effect on ATPase in the presence of other divalent cations, Mg
2+-ATPase being more sensitive to Cd
2+ than Ca
2+-ATPase. The inhibition of Mg
2+-ATPase was competitive at 10°C and 4°C but not at higher temperatures.
6.
6. Some of the toxic effects of Cd
2+ on the
Anodonta gill ATPase at ecological temperatures are probably due to competition for Mg
2+ binding sites.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/0306-4565(95)00025-9</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of thermal biology, 1996, Vol.21 (2), p.77-84 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_15655107 |
| source | Elsevier ScienceDirect Journals |
| subjects | Anodonta cygnea ATPases cadmium Freshwater gills molluscs temperature |
| title | Effect of cadmium on the ATPase activity in gills of Anodonta cygnea at different assay temperatures |
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