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Publication Type
Journal Article
UWI Author(s)
Author, Analytic
Bennett, Franklyn I.; Jackson, Alan A.
Author Affiliation, Ana.
Pathology
Article Title
Glycine is not formed through the amino transferase reaction in human or rat placenta.
Medium Designator
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Connective Phrase
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Journal Title
Placenta
Translated Title
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Reprint Status
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Date of Publication
1998
Volume ID
19
Issue ID
3
Page(s)
21-31
Language
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Connective Phrase
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Location/URL
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ISSN
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Notes
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Abstract
The fetus has a substantial demand for glycine, which is satisfied in part by placental formation. The ability to form glycine through the activity of alanine: gloxylate aminotransferase enzyme was measured in placentae from normal term human pregnancies and placentae from rats at day 20 of gestation. There was no detectable enzyme activity in either human or rat placentae, although activity was measured in rat liver. It is concluded that in the placenta glycine is only formed from serine through the activity of serine hydroxymethyl transferase enzyme, which uses folate as a cofactor, because there is no other known metabolic pathway for endogenous glycine production.....
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Keywords
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