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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1977-6-30
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pubmed:abstractText |
This and previous papers examine the reasons for the relationship between the concentrations of guanidino-succinate and guanidinoacetate in human urine. With the demonstration here that extracts of human liver-tissue can mediate ureidohomoserine formation from canaline [(2-amino-4-aminooxy)-butyric acid] and carbamoyl phosphate, all steps in a cycle proposed for the production of guanidinoacetate and guanidinosuccinate have been documented. This includes synthesis of canavaninosuccinate from aspartate and ureidohomoserine, reductive cleavage of canavaninosuccinate to form guanidinosuccinate and homoserine, or, alternatively, lytic action on canavaninosuccinate to form fumarate and canavanine, and transamidination to glycine to form guanidinoacetate, regenerating the canaline. We propose that canaline originates from aspartate, but the precise mechanism by which canaline is formed needs to be elucidated.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0009-9147
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
960-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15744-Aminobutyric Acids,
pubmed-meshheading:15744-Chromatography, Gel,
pubmed-meshheading:15744-Guanidines,
pubmed-meshheading:15744-Humans,
pubmed-meshheading:15744-Hydrogen-Ion Concentration,
pubmed-meshheading:15744-Kinetics,
pubmed-meshheading:15744-Liver,
pubmed-meshheading:15744-Methods,
pubmed-meshheading:15744-Ornithine Carbamoyltransferase,
pubmed-meshheading:15744-Transferases
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pubmed:year |
1977
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pubmed:articleTitle |
Canaline carbamoyltransferase in human liver as part of a metabolic cycle in which guanidino compounds are formed.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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