Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei
We have cloned two genes ( aldo-1 and aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1992-05, Vol.52 (1), p.15-27 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Meier, Bea Döbeli, Heinz Certa, Ulrich |
| description | We have cloned two genes (
aldo-1 and
aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite
Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to
P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in
Escherichia coli and compared the biochemical and kinetic properties to that of
P. falciparum recombinant aldolase (ALDO-1 type). Based on the
K
m and
V
max constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of
P. berghei and ALDO-2 is found in blood stage parasites. |
| doi_str_mv | 10.1016/0166-6851(92)90032-F |
| format | Article |
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aldo-1 and
aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite
Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to
P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in
Escherichia coli and compared the biochemical and kinetic properties to that of
P. falciparum recombinant aldolase (ALDO-1 type). Based on the
K
m and
V
max constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of
P. berghei and ALDO-2 is found in blood stage parasites.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(92)90032-F</identifier><identifier>PMID: 1625704</identifier><identifier>CODEN: MBIPDP</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>Aldolase isoenzyme ; Amino Acid Sequence ; Animals ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Biological Evolution ; Blotting, Western ; Cloning, Molecular ; Evolution ; Fructose-Bisphosphate Aldolase - biosynthesis ; Fructose-Bisphosphate Aldolase - genetics ; Fructose-Bisphosphate Aldolase - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycolysis ; Humans ; Isoenzymes - biosynthesis ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Kinetics ; Molecular Sequence Data ; Plasmodium berghei ; Plasmodium berghei - enzymology ; Plasmodium berghei - genetics ; Plasmodium berghei - growth & development ; Protozoa ; Restriction Mapping ; Sequence Alignment ; Substrate Specificity ; Tropical medicine</subject><ispartof>Molecular and biochemical parasitology, 1992-05, Vol.52 (1), p.15-27</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-5f430cb7fca2bb2789901ec1ea33e22d8cc754781c24094ea081ae9c36f8b35e3</citedby><cites>FETCH-LOGICAL-c417t-5f430cb7fca2bb2789901ec1ea33e22d8cc754781c24094ea081ae9c36f8b35e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/016668519290032F$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5351977$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1625704$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meier, Bea</creatorcontrib><creatorcontrib>Döbeli, Heinz</creatorcontrib><creatorcontrib>Certa, Ulrich</creatorcontrib><title>Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>We have cloned two genes (
aldo-1 and
aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite
Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to
P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in
Escherichia coli and compared the biochemical and kinetic properties to that of
P. falciparum recombinant aldolase (ALDO-1 type). Based on the
K
m and
V
max constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of
P. berghei and ALDO-2 is found in blood stage parasites.</description><subject>Aldolase isoenzyme</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Biological Evolution</subject><subject>Blotting, Western</subject><subject>Cloning, Molecular</subject><subject>Evolution</subject><subject>Fructose-Bisphosphate Aldolase - biosynthesis</subject><subject>Fructose-Bisphosphate Aldolase - genetics</subject><subject>Fructose-Bisphosphate Aldolase - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycolysis</subject><subject>Humans</subject><subject>Isoenzymes - biosynthesis</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Plasmodium berghei</subject><subject>Plasmodium berghei - enzymology</subject><subject>Plasmodium berghei - genetics</subject><subject>Plasmodium berghei - growth & development</subject><subject>Protozoa</subject><subject>Restriction Mapping</subject><subject>Sequence Alignment</subject><subject>Substrate Specificity</subject><subject>Tropical medicine</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EKkvhH4DkA6rgEPBHbMcXJFSxUKkSSMDZmjiT1iiJgyeLWn49WXZVbuUwmsM8Mxo9L2PPpXgjhbRv17KVbYx85dVrL4RW1fYB28jGqcrXqnnINnfIY_aE6IcQwjhrT9iJtMo4UW9Y-3WBK6xoxpj6FDnezAWJUp547jkMXR6AkCfKOP2-HZF4mvhyjbzkDqeFjzBAScBnKEBpQf5l5cfcpd3IWyxX15ieskc9DITPjv2Ufd9--Hb-qbr8_PHi_P1lFWvplsr0tRaxdX0E1bbKNd4LiVEiaI1KdU2MztSukVHVwtcIopGAPmrbN602qE_Z2eHuXPLPHdISxkQRhwEmzDsKTgsrtFT_BVdp0gpnVrA-gLFkooJ9mEsaodwGKcI-g7AXHPaCg1fhbwZhu669ON7ftSN2_5YO0tf5y-McKMLQF5hiojvMaCO9cyv27oDhKu1XwhIoJpwidqlgXEKX0_1__AF3gqOe</recordid><startdate>19920501</startdate><enddate>19920501</enddate><creator>Meier, Bea</creator><creator>Döbeli, Heinz</creator><creator>Certa, Ulrich</creator><general>Elsevier B.V</general><general>Elsevier Science</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19920501</creationdate><title>Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei</title><author>Meier, Bea ; Döbeli, Heinz ; Certa, Ulrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-5f430cb7fca2bb2789901ec1ea33e22d8cc754781c24094ea081ae9c36f8b35e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Aldolase isoenzyme</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Biological Evolution</topic><topic>Blotting, Western</topic><topic>Cloning, Molecular</topic><topic>Evolution</topic><topic>Fructose-Bisphosphate Aldolase - biosynthesis</topic><topic>Fructose-Bisphosphate Aldolase - genetics</topic><topic>Fructose-Bisphosphate Aldolase - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycolysis</topic><topic>Humans</topic><topic>Isoenzymes - biosynthesis</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Plasmodium berghei</topic><topic>Plasmodium berghei - enzymology</topic><topic>Plasmodium berghei - genetics</topic><topic>Plasmodium berghei - growth & development</topic><topic>Protozoa</topic><topic>Restriction Mapping</topic><topic>Sequence Alignment</topic><topic>Substrate Specificity</topic><topic>Tropical medicine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meier, Bea</creatorcontrib><creatorcontrib>Döbeli, Heinz</creatorcontrib><creatorcontrib>Certa, Ulrich</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meier, Bea</au><au>Döbeli, Heinz</au><au>Certa, Ulrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1992-05-01</date><risdate>1992</risdate><volume>52</volume><issue>1</issue><spage>15</spage><epage>27</epage><pages>15-27</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><coden>MBIPDP</coden><abstract>We have cloned two genes (
aldo-1 and
aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite
Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to
P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in
Escherichia coli and compared the biochemical and kinetic properties to that of
P. falciparum recombinant aldolase (ALDO-1 type). Based on the
K
m and
V
max constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of
P. berghei and ALDO-2 is found in blood stage parasites.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>1625704</pmid><doi>10.1016/0166-6851(92)90032-F</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Molecular and biochemical parasitology, 1992-05, Vol.52 (1), p.15-27 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Aldolase isoenzyme Amino Acid Sequence Animals Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Biological Evolution Blotting, Western Cloning, Molecular Evolution Fructose-Bisphosphate Aldolase - biosynthesis Fructose-Bisphosphate Aldolase - genetics Fructose-Bisphosphate Aldolase - metabolism Fundamental and applied biological sciences. Psychology Glycolysis Humans Isoenzymes - biosynthesis Isoenzymes - genetics Isoenzymes - metabolism Kinetics Molecular Sequence Data Plasmodium berghei Plasmodium berghei - enzymology Plasmodium berghei - genetics Plasmodium berghei - growth & development Protozoa Restriction Mapping Sequence Alignment Substrate Specificity Tropical medicine |
| title | Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei |
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