Loading…
Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti
Isocitrate lyase from both young and old free living nematodes (Turbatrix aceti) has been purified and compared. The "old" enzyme consists of the same five isozymes as the "young" preparation, but with quantitative differences. The enzyme shows an age-related decline in specific...
Saved in:
| Published in: | The Journal of biological chemistry 1975-02, Vol.250 (3), p.826-830 |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23 |
| container_end_page | 830 |
| container_issue | 3 |
| container_start_page | 826 |
| container_title | The Journal of biological chemistry |
| container_volume | 250 |
| creator | Reiss, U Rothstein, M |
| description | Isocitrate lyase from both young and old free living nematodes (Turbatrix aceti) has been purified and compared. The "old"
enzyme consists of the same five isozymes as the "young" preparation, but with quantitative differences. The enzyme shows
an age-related decline in specific activity. Use of antibodies has confirmed the accumulation of cross-reacting material in
old organisms as found by Gershon and Gershon ((1970) Nature 227, 1214), using crude homogenates. Km, molecular weight, subunit
size, and behavior toward the inhibitors oxalate, malonate, and tartronate all appear unchanged. Although the enzyme isolated
from old organisms has a sharply reduced specific activity, it binds as well to an affinity column as does "young" enzyme.
It is tentatively concluded that the loss of specific activity in the "old" enzyme is due to the presence of partially active
molecules, rather than to a mixture of active and inactive molecules. |
| doi_str_mv | 10.1016/S0021-9258(19)41859-0 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82741125</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>82741125</sourcerecordid><originalsourceid>FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23</originalsourceid><addsrcrecordid>eNo9kFlLxDAQx4N4ravfQCG-iILVSdI2zaOIFyz44IFvIU2m20gPTboe396uK87LXP__DPwIOWBwxoDl5w8AnCWKZ8UxUycpKzKVwBqZMChEIjL2sk4m_5JtshPjK4yRKrZFNgsQGcCEPF_MMQnYmAEdtbXp5hip76iPvfVDGMe0-TYRaRX6lg71ssBx5j98N6cdtmboHZ7Sx0UozRD8FzUWB79LNirTRNz7y1PydH31eHmbzO5v7i4vZokVMh8SJ3PpSpmhdFyUaFJnCwmVUyhUxUoFyw6t4y6XCquSSUhLy1MsUptDxcWUHK3uvoX-fYFx0K2PFpvGdNgvoi64TBnj2SjMVkIb-hgDVvot-NaEb81AL3HqX5x6yUozpX9xahh9-38PFmWL7t-14jeuD1fr2s_rTx9Ql763NbaaZ6DF-D8XP7YbfFY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82741125</pqid></control><display><type>article</type><title>Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti</title><source>ScienceDirect</source><creator>Reiss, U ; Rothstein, M</creator><creatorcontrib>Reiss, U ; Rothstein, M</creatorcontrib><description>Isocitrate lyase from both young and old free living nematodes (Turbatrix aceti) has been purified and compared. The "old"
enzyme consists of the same five isozymes as the "young" preparation, but with quantitative differences. The enzyme shows
an age-related decline in specific activity. Use of antibodies has confirmed the accumulation of cross-reacting material in
old organisms as found by Gershon and Gershon ((1970) Nature 227, 1214), using crude homogenates. Km, molecular weight, subunit
size, and behavior toward the inhibitors oxalate, malonate, and tartronate all appear unchanged. Although the enzyme isolated
from old organisms has a sharply reduced specific activity, it binds as well to an affinity column as does "young" enzyme.
It is tentatively concluded that the loss of specific activity in the "old" enzyme is due to the presence of partially active
molecules, rather than to a mixture of active and inactive molecules.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)41859-0</identifier><identifier>PMID: 803500</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Aging ; Animals ; Chromatography, Affinity ; Cold Temperature ; Drug Stability ; Immunodiffusion ; Isocitrates ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Kinetics ; Macromolecular Substances ; Molecular Weight ; Nematoda - enzymology ; Oxalates - pharmacology ; Oxo-Acid-Lyases - immunology ; Oxo-Acid-Lyases - isolation & purification ; Oxo-Acid-Lyases - metabolism ; Precipitin Tests ; Time Factors</subject><ispartof>The Journal of biological chemistry, 1975-02, Vol.250 (3), p.826-830</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23</citedby><cites>FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23</cites></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/803500$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reiss, U</creatorcontrib><creatorcontrib>Rothstein, M</creatorcontrib><title>Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Isocitrate lyase from both young and old free living nematodes (Turbatrix aceti) has been purified and compared. The "old"
enzyme consists of the same five isozymes as the "young" preparation, but with quantitative differences. The enzyme shows
an age-related decline in specific activity. Use of antibodies has confirmed the accumulation of cross-reacting material in
old organisms as found by Gershon and Gershon ((1970) Nature 227, 1214), using crude homogenates. Km, molecular weight, subunit
size, and behavior toward the inhibitors oxalate, malonate, and tartronate all appear unchanged. Although the enzyme isolated
from old organisms has a sharply reduced specific activity, it binds as well to an affinity column as does "young" enzyme.
It is tentatively concluded that the loss of specific activity in the "old" enzyme is due to the presence of partially active
molecules, rather than to a mixture of active and inactive molecules.</description><subject>Aging</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Cold Temperature</subject><subject>Drug Stability</subject><subject>Immunodiffusion</subject><subject>Isocitrates</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Nematoda - enzymology</subject><subject>Oxalates - pharmacology</subject><subject>Oxo-Acid-Lyases - immunology</subject><subject>Oxo-Acid-Lyases - isolation & purification</subject><subject>Oxo-Acid-Lyases - metabolism</subject><subject>Precipitin Tests</subject><subject>Time Factors</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><recordid>eNo9kFlLxDAQx4N4ravfQCG-iILVSdI2zaOIFyz44IFvIU2m20gPTboe396uK87LXP__DPwIOWBwxoDl5w8AnCWKZ8UxUycpKzKVwBqZMChEIjL2sk4m_5JtshPjK4yRKrZFNgsQGcCEPF_MMQnYmAEdtbXp5hip76iPvfVDGMe0-TYRaRX6lg71ssBx5j98N6cdtmboHZ7Sx0UozRD8FzUWB79LNirTRNz7y1PydH31eHmbzO5v7i4vZokVMh8SJ3PpSpmhdFyUaFJnCwmVUyhUxUoFyw6t4y6XCquSSUhLy1MsUptDxcWUHK3uvoX-fYFx0K2PFpvGdNgvoi64TBnj2SjMVkIb-hgDVvot-NaEb81AL3HqX5x6yUozpX9xahh9-38PFmWL7t-14jeuD1fr2s_rTx9Ql763NbaaZ6DF-D8XP7YbfFY</recordid><startdate>19750210</startdate><enddate>19750210</enddate><creator>Reiss, U</creator><creator>Rothstein, M</creator><general>American Society for Biochemistry and Molecular Biology</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>19750210</creationdate><title>Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti</title><author>Reiss, U ; Rothstein, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Aging</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Cold Temperature</topic><topic>Drug Stability</topic><topic>Immunodiffusion</topic><topic>Isocitrates</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Nematoda - enzymology</topic><topic>Oxalates - pharmacology</topic><topic>Oxo-Acid-Lyases - immunology</topic><topic>Oxo-Acid-Lyases - isolation & purification</topic><topic>Oxo-Acid-Lyases - metabolism</topic><topic>Precipitin Tests</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reiss, U</creatorcontrib><creatorcontrib>Rothstein, M</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reiss, U</au><au>Rothstein, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1975-02-10</date><risdate>1975</risdate><volume>250</volume><issue>3</issue><spage>826</spage><epage>830</epage><pages>826-830</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Isocitrate lyase from both young and old free living nematodes (Turbatrix aceti) has been purified and compared. The "old"
enzyme consists of the same five isozymes as the "young" preparation, but with quantitative differences. The enzyme shows
an age-related decline in specific activity. Use of antibodies has confirmed the accumulation of cross-reacting material in
old organisms as found by Gershon and Gershon ((1970) Nature 227, 1214), using crude homogenates. Km, molecular weight, subunit
size, and behavior toward the inhibitors oxalate, malonate, and tartronate all appear unchanged. Although the enzyme isolated
from old organisms has a sharply reduced specific activity, it binds as well to an affinity column as does "young" enzyme.
It is tentatively concluded that the loss of specific activity in the "old" enzyme is due to the presence of partially active
molecules, rather than to a mixture of active and inactive molecules.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>803500</pmid><doi>10.1016/S0021-9258(19)41859-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1975-02, Vol.250 (3), p.826-830 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82741125 |
| source | ScienceDirect |
| subjects | Aging Animals Chromatography, Affinity Cold Temperature Drug Stability Immunodiffusion Isocitrates Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Macromolecular Substances Molecular Weight Nematoda - enzymology Oxalates - pharmacology Oxo-Acid-Lyases - immunology Oxo-Acid-Lyases - isolation & purification Oxo-Acid-Lyases - metabolism Precipitin Tests Time Factors |
| title | Age-related changes in isocitrate lyase from the free living nematode, Turbatrix aceti |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T04%3A47%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Age-related%20changes%20in%20isocitrate%20lyase%20from%20the%20free%20living%20nematode,%20Turbatrix%20aceti&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Reiss,%20U&rft.date=1975-02-10&rft.volume=250&rft.issue=3&rft.spage=826&rft.epage=830&rft.pages=826-830&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(19)41859-0&rft_dat=%3Cproquest_cross%3E82741125%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c376t-d767db75e7d23bea4dc870fd9e39f1b90870fecd2d679efb1704bc24e84c60f23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=82741125&rft_id=info:pmid/803500&rfr_iscdi=true |