TY - JOUR
T1 - Comparative and developmental studies on 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase
AU - Gregory, Kathleen
AU - Carnie, J. A.
AU - Rowsell, E. V.
AU - Dabbaghian, Maral K.
AU - Hobbs, D. R.
AU - Rowsell, Kathleen V.
PY - 1982
Y1 - 1982
N2 - 1. 1. In rats, liver 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase activities are maximal in the suckling period. 2. 2. Liver activities for 4-hydroxy-2-oxoglutarate aldolase, alanine-glyoxylate aminotransferase, serine-pyruvate aminotransferase and serine dehydratase, but not hydroxyproline oxidase, are increased in rats on a high-fat, carbohydrate-free diet. 3. 3. It is suggested that 4-hydroxy-2-oxoglutarate may be a significant source of glyoxylate for glycine and hence glucose formation. 4. 4. Mammalian liver hydroxyproline oxidase activity is higher in carnivorous species; necessary, perhaps, to metabolise a relatively large influx of hydroxyproline on a flesh diet. © 1982.
AB - 1. 1. In rats, liver 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase activities are maximal in the suckling period. 2. 2. Liver activities for 4-hydroxy-2-oxoglutarate aldolase, alanine-glyoxylate aminotransferase, serine-pyruvate aminotransferase and serine dehydratase, but not hydroxyproline oxidase, are increased in rats on a high-fat, carbohydrate-free diet. 3. 3. It is suggested that 4-hydroxy-2-oxoglutarate may be a significant source of glyoxylate for glycine and hence glucose formation. 4. 4. Mammalian liver hydroxyproline oxidase activity is higher in carnivorous species; necessary, perhaps, to metabolise a relatively large influx of hydroxyproline on a flesh diet. © 1982.
M3 - Article
C2 - 0007083820
SN - 0305-0491
VL - 71
SP - 681
EP - 687
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
IS - 4
ER -