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Effect of cobalamin inactivation on folate-dependent transformylases involved in purine synthesis in rats

Authors :
Deacon, R
Perry, J
Lumb, M
Chanarin, I
Source :
Biochemical Journal; April 1985, Vol. 227 Issue: 1 p67-71, 5p
Publication Year :
1985

Abstract

N2O oxidizes and inactivates cob[I]alamin, and animals exposed in this way serve as models for cobalamin ‘deficiency’. Such animals show a fall in activity of glycinamide ribotide transformylase and a rise in that of 5-amino-4-imidazolecarboxamide ribotide transformylase. The fall in glycinamide ribotide transformylase activity was prevented by parenteral 5'-methylthioadenosine derived from methionine. Methylthioadenosine in turn is converted into formate. Activity of glycinamide ribotide transformylase recovers after 7 days despite continued N2O inhalation, and this is probably related to restoration of methionine synthesis by induction of betaine:homocysteine transmethylase.

Details

Language :
English
ISSN :
02646021 and 14708728
Volume :
227
Issue :
1
Database :
Supplemental Index
Journal :
Biochemical Journal
Publication Type :
Periodical
Accession number :
ejs51298032
Full Text :
https://doi.org/10.1042/bj2270067