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Studies with tryptophan metabolites in vitro: Kynurenine metabolism in liver homogenates of normal and
The conversion of kynurenine into kynurenic acid and anthranilic acid in both normal and Schistosoma mansoni -infested mouse liver was investigated. It was found that in the S. mansoni -infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynur...
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| Published in: | Biochemical journal 1967-08, Vol.104 (2), p.656-662 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 662 |
| container_issue | 2 |
| container_start_page | 656 |
| container_title | Biochemical journal |
| container_volume | 104 |
| creator | Amer, M. Samir Abdel-Daim, M. H. Abdel-Tawab, G. A. |
| description | The conversion of kynurenine into kynurenic acid and anthranilic acid in both normal and
Schistosoma mansoni
-infested mouse liver was investigated. It was found that in the
S. mansoni
-infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynurenine transaminase and a low production of kynurenic acid. Deoxypyridoxine and its phosphorylated derivative inhibited kynurenine transaminase in the normal liver in a pattern qualitatively similar to that observed with infested liver. The lowered concentration of pyridoxal phosphate in the infested liver is discussed in view of the possibility of two combined mechanisms: (
a
) an antimetabolite being secreted by the infesting worms or present in its eggs that partially inhibited the phosphorylation of pyridoxal, and (
b
) concentration of pyridoxal phosphate by the worms, resulting in a lowered concentration of the cofactor in the host tissue. |
| format | article |
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Schistosoma mansoni
-infested mouse liver was investigated. It was found that in the
S. mansoni
-infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynurenine transaminase and a low production of kynurenic acid. Deoxypyridoxine and its phosphorylated derivative inhibited kynurenine transaminase in the normal liver in a pattern qualitatively similar to that observed with infested liver. The lowered concentration of pyridoxal phosphate in the infested liver is discussed in view of the possibility of two combined mechanisms: (
a
) an antimetabolite being secreted by the infesting worms or present in its eggs that partially inhibited the phosphorylation of pyridoxal, and (
b
) concentration of pyridoxal phosphate by the worms, resulting in a lowered concentration of the cofactor in the host tissue.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>PMID: 6048805</identifier><language>eng</language><ispartof>Biochemical journal, 1967-08, Vol.104 (2), p.656-662</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1270633/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1270633/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,53769,53771</link.rule.ids></links><search><creatorcontrib>Amer, M. Samir</creatorcontrib><creatorcontrib>Abdel-Daim, M. H.</creatorcontrib><creatorcontrib>Abdel-Tawab, G. A.</creatorcontrib><title>Studies with tryptophan metabolites in vitro: Kynurenine metabolism in liver homogenates of normal and</title><title>Biochemical journal</title><description>The conversion of kynurenine into kynurenic acid and anthranilic acid in both normal and
Schistosoma mansoni
-infested mouse liver was investigated. It was found that in the
S. mansoni
-infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynurenine transaminase and a low production of kynurenic acid. Deoxypyridoxine and its phosphorylated derivative inhibited kynurenine transaminase in the normal liver in a pattern qualitatively similar to that observed with infested liver. The lowered concentration of pyridoxal phosphate in the infested liver is discussed in view of the possibility of two combined mechanisms: (
a
) an antimetabolite being secreted by the infesting worms or present in its eggs that partially inhibited the phosphorylation of pyridoxal, and (
b
) concentration of pyridoxal phosphate by the worms, resulting in a lowered concentration of the cofactor in the host tissue.</description><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1967</creationdate><recordtype>article</recordtype><recordid>eNqlzLsOwiAYQGFiNLVe3oEHsMkPRcrkYjTuuhNq0WJaIEBrfHsdXJydzvAlZ4JywiooREXFFOVAOSs4UDJHixgfAIQBgwxlHJgQsM3R5pyGxuiInya1OIWXT863yuJeJ1W7zqSPGYtHk4JbodlNdVGvv12i3fFw2Z8KP9S9bq7apqA66YPpVXhJp4z8FWtaeXejJLQCXpbl34M3TLlMGw</recordid><startdate>19670801</startdate><enddate>19670801</enddate><creator>Amer, M. Samir</creator><creator>Abdel-Daim, M. H.</creator><creator>Abdel-Tawab, G. A.</creator><scope>5PM</scope></search><sort><creationdate>19670801</creationdate><title>Studies with tryptophan metabolites in vitro</title><author>Amer, M. Samir ; Abdel-Daim, M. H. ; Abdel-Tawab, G. A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmedcentral_primary_oai_pubmedcentral_nih_gov_12706333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1967</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amer, M. Samir</creatorcontrib><creatorcontrib>Abdel-Daim, M. H.</creatorcontrib><creatorcontrib>Abdel-Tawab, G. A.</creatorcontrib><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amer, M. Samir</au><au>Abdel-Daim, M. H.</au><au>Abdel-Tawab, G. A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies with tryptophan metabolites in vitro: Kynurenine metabolism in liver homogenates of normal and</atitle><jtitle>Biochemical journal</jtitle><date>1967-08-01</date><risdate>1967</risdate><volume>104</volume><issue>2</issue><spage>656</spage><epage>662</epage><pages>656-662</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The conversion of kynurenine into kynurenic acid and anthranilic acid in both normal and
Schistosoma mansoni
-infested mouse liver was investigated. It was found that in the
S. mansoni
-infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynurenine transaminase and a low production of kynurenic acid. Deoxypyridoxine and its phosphorylated derivative inhibited kynurenine transaminase in the normal liver in a pattern qualitatively similar to that observed with infested liver. The lowered concentration of pyridoxal phosphate in the infested liver is discussed in view of the possibility of two combined mechanisms: (
a
) an antimetabolite being secreted by the infesting worms or present in its eggs that partially inhibited the phosphorylation of pyridoxal, and (
b
) concentration of pyridoxal phosphate by the worms, resulting in a lowered concentration of the cofactor in the host tissue.</abstract><pmid>6048805</pmid></addata></record> |
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| ispartof | Biochemical journal, 1967-08, Vol.104 (2), p.656-662 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | PubMed Central |
| title | Studies with tryptophan metabolites in vitro: Kynurenine metabolism in liver homogenates of normal and |
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