Trypanosoma (Nannomonas) congolense: properties of hexokinase and phosphofructokinase from cultured procyclic trypomastigotes and bloodstream forms
The distribution and kinetics of two key glycolytic enzymes hexokinase (HK) and phosphofructokinase (PFK) were studied in animal-infective bloodstream forms (haematozoic trypomastigotes) and uninfective procyclic forms (insect trypomastigotes) of Trypanosoma congolense. The results show that in both...
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| Veröffentlicht in: | Acta tropica 1987-09, Vol.44 (3), p.283-292 |
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| creator | NWAGWU, M HIRUMI, H |
| description | The distribution and kinetics of two key glycolytic enzymes hexokinase (HK) and phosphofructokinase (PFK) were studied in animal-infective bloodstream forms (haematozoic trypomastigotes) and uninfective procyclic forms (insect trypomastigotes) of Trypanosoma congolense. The results show that in both forms of T. congolense HK and PFK are particulate and are probably localized in a membrane-delimited organelle, the glycosome. Hexokinases of bloodstream and procyclic forms of T. congolense are kinetically similar with respect to their affinity for glucose and ATP, the apparent Km for glucose being within the range, of 91 microM to 100 microM and that for ATP, 65 microM to 91 microM. Phosphofructokinase of both forms responds to its substrate in a complex manner: a plot of initial velocity versus substrate concentration displays intermediary plateau regions. |
| format | Article |
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The results show that in both forms of T. congolense HK and PFK are particulate and are probably localized in a membrane-delimited organelle, the glycosome. Hexokinases of bloodstream and procyclic forms of T. congolense are kinetically similar with respect to their affinity for glucose and ATP, the apparent Km for glucose being within the range, of 91 microM to 100 microM and that for ATP, 65 microM to 91 microM. Phosphofructokinase of both forms responds to its substrate in a complex manner: a plot of initial velocity versus substrate concentration displays intermediary plateau regions.</description><identifier>ISSN: 0001-706X</identifier><identifier>EISSN: 1873-6254</identifier><identifier>PMID: 2892364</identifier><identifier>CODEN: ACTRAQ</identifier><language>eng</language><publisher>Amsterdam: Elsevier</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Biological and medical sciences ; Glucose - metabolism ; Hexokinase - metabolism ; Human protozoal diseases ; Infectious diseases ; Kinetics ; Medical sciences ; Parasitic diseases ; Phosphofructokinase-1 - metabolism ; Protozoal diseases ; Tropical medicine ; Trypanosoma congolense - enzymology ; Trypanosomiasis</subject><ispartof>Acta tropica, 1987-09, Vol.44 (3), p.283-292</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7460677$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2892364$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>NWAGWU, M</creatorcontrib><creatorcontrib>HIRUMI, H</creatorcontrib><title>Trypanosoma (Nannomonas) congolense: properties of hexokinase and phosphofructokinase from cultured procyclic trypomastigotes and bloodstream forms</title><title>Acta tropica</title><addtitle>Acta Trop</addtitle><description>The distribution and kinetics of two key glycolytic enzymes hexokinase (HK) and phosphofructokinase (PFK) were studied in animal-infective bloodstream forms (haematozoic trypomastigotes) and uninfective procyclic forms (insect trypomastigotes) of Trypanosoma congolense. The results show that in both forms of T. congolense HK and PFK are particulate and are probably localized in a membrane-delimited organelle, the glycosome. Hexokinases of bloodstream and procyclic forms of T. congolense are kinetically similar with respect to their affinity for glucose and ATP, the apparent Km for glucose being within the range, of 91 microM to 100 microM and that for ATP, 65 microM to 91 microM. Phosphofructokinase of both forms responds to its substrate in a complex manner: a plot of initial velocity versus substrate concentration displays intermediary plateau regions.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Glucose - metabolism</subject><subject>Hexokinase - metabolism</subject><subject>Human protozoal diseases</subject><subject>Infectious diseases</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Parasitic diseases</subject><subject>Phosphofructokinase-1 - metabolism</subject><subject>Protozoal diseases</subject><subject>Tropical medicine</subject><subject>Trypanosoma congolense - enzymology</subject><subject>Trypanosomiasis</subject><issn>0001-706X</issn><issn>1873-6254</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9UE1LxDAQDaKs6-pPEHIQ0UMhbZom600Wv2DRywreSppMdqttUpMU3N_hHzaLq4dhmHlv3puZAzTNBadZVbDyEE0JIXnGSfV2jE5CeE9VwVkxQZNCzAtalVP0vfLbQVoXXC_x1bO01vXOynCNlbNr14ENcIMH7wbwsYWAncEb-HIfbSIBllbjYeNCCuNHFf_6xrseq7GLowe9G1db1bUKx-SWnEJs1y4mtd180zmnQ_Qge2yc78MpOjKyC3C2zzP0en-3Wjxmy5eHp8XtMhtyRmLGFTWiqCiVBjSTOidQVIxqwRqlCNNCgDCclUJV6VzDtFGsAZ3rOSOaUEVn6PJXN-33OUKIdd8GBV0nLbgx1JwLIVhJEvF8TxybHnQ9-LaXflvvv5jwiz0ug5Kd8dKqNvzTeFmRinP6A4nRgak</recordid><startdate>198709</startdate><enddate>198709</enddate><creator>NWAGWU, M</creator><creator>HIRUMI, H</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198709</creationdate><title>Trypanosoma (Nannomonas) congolense: properties of hexokinase and phosphofructokinase from cultured procyclic trypomastigotes and bloodstream forms</title><author>NWAGWU, M ; HIRUMI, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p150t-7c3f82633afed5ad10e2653d85bcc05d88e8f7548c6289f5dfc5bed1d950d03c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Glucose - metabolism</topic><topic>Hexokinase - metabolism</topic><topic>Human protozoal diseases</topic><topic>Infectious diseases</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Parasitic diseases</topic><topic>Phosphofructokinase-1 - metabolism</topic><topic>Protozoal diseases</topic><topic>Tropical medicine</topic><topic>Trypanosoma congolense - enzymology</topic><topic>Trypanosomiasis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NWAGWU, M</creatorcontrib><creatorcontrib>HIRUMI, H</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>MEDLINE - Academic</collection><jtitle>Acta tropica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>NWAGWU, M</au><au>HIRUMI, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trypanosoma (Nannomonas) congolense: properties of hexokinase and phosphofructokinase from cultured procyclic trypomastigotes and bloodstream forms</atitle><jtitle>Acta tropica</jtitle><addtitle>Acta Trop</addtitle><date>1987-09</date><risdate>1987</risdate><volume>44</volume><issue>3</issue><spage>283</spage><epage>292</epage><pages>283-292</pages><issn>0001-706X</issn><eissn>1873-6254</eissn><coden>ACTRAQ</coden><abstract>The distribution and kinetics of two key glycolytic enzymes hexokinase (HK) and phosphofructokinase (PFK) were studied in animal-infective bloodstream forms (haematozoic trypomastigotes) and uninfective procyclic forms (insect trypomastigotes) of Trypanosoma congolense. The results show that in both forms of T. congolense HK and PFK are particulate and are probably localized in a membrane-delimited organelle, the glycosome. Hexokinases of bloodstream and procyclic forms of T. congolense are kinetically similar with respect to their affinity for glucose and ATP, the apparent Km for glucose being within the range, of 91 microM to 100 microM and that for ATP, 65 microM to 91 microM. Phosphofructokinase of both forms responds to its substrate in a complex manner: a plot of initial velocity versus substrate concentration displays intermediary plateau regions.</abstract><cop>Amsterdam</cop><pub>Elsevier</pub><pmid>2892364</pmid><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0001-706X |
| ispartof | Acta tropica, 1987-09, Vol.44 (3), p.283-292 |
| issn | 0001-706X 1873-6254 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77888540 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; e-periodica |
| subjects | Adenosine Triphosphate - metabolism Animals Biological and medical sciences Glucose - metabolism Hexokinase - metabolism Human protozoal diseases Infectious diseases Kinetics Medical sciences Parasitic diseases Phosphofructokinase-1 - metabolism Protozoal diseases Tropical medicine Trypanosoma congolense - enzymology Trypanosomiasis |
| title | Trypanosoma (Nannomonas) congolense: properties of hexokinase and phosphofructokinase from cultured procyclic trypomastigotes and bloodstream forms |
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