Abstract
1. The highest blood concentrations of ketone bodies were found at 5 days of age, after which time the concentration fell to reach the adult value by 30 days of age. 2. Both mitochondrial and cytoplasmic hydroxymethylglutaryl-CoA synthase activities were detected, with highest activities being found in the mitochondria at all stages of development. Activity of the mitochondrial enzyme increases rapidly immediately after birth, showing a maximum at 15 days of age, thereafter falling to adult values. The cytoplasmic enzyme, on the other hand, increased steadily in activity after birth to reach a maximum at 40 days of age, after which time activity fell to adult values. 3. Both mitochondrial and cytoplasmic aceto-acetyl-CoA thiolase activities were detected, with the mitochondrial enzyme having considerably higher activities at all stages of development. The developmental patterns for both enzymes were very similar to those for the corresponding hydroxymethylglutaryl-CoA synthases. 4. The activity of heart acetoacetyl-CoA transferase remains constant from late foetal life until the end of the suckling period, after which time there is a gradual threefold increase in activity to reach the adult values. The activity of brain 3-oxo acid CoA-transferase increases steadily after birth, reaching a maximum at 30 days of age, thereafter decreasing to adult values, which are similar to foetal activities. Although at all stages of development the specific activity of the heart enzyme is higher than that of brain, the total enzymic capacity of the brain is higher than that of the heart during the suckling period.
MeSH Terms
Acidosis/metabolism
Acyltransferases/metabolism
Age Factors
Animals
Animals, Newborn
Brain/enzymology
Cytoplasm/enzymology
Fetus/enzymology
Growth
Ketone Bodies/metabolism
Ketones/biosynthesis,blood
Lyases
Mitochondria/enzymology
Myocardium/enzymology
Rats
Chemicals
Ketone Bodies
Ketones
Acyltransferases
Lyases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lockwood E A
Bailey E
References (16)
16 references, click to expand
-
Changes in hepatic lipigenesis during development of the rat.
Biochem J. 1967 Nov;105(2):717-22
PMID: 4296324
-
Acetoacetate formation by liver slices from adult and infant rats.
Biochem J. 1964 Oct;93(1):61-5
PMID: 5838104
-
Factors involved in changes in hepatic lipogenesis during development of the rat.
Biochem J. 1970 Jun;118(1):155-62
PMID: 4248618
-
Development of gluconeogenesis in neonatal rat liver. Effect of triamcinolone.
Biochem J. 1967 Dec;105(3):1219-27
PMID: 16742549
-
Activity and intracellular distribution of enzymes of ketone-body metabolism in rat liver.
Biochem J. 1968 Jul;108(3):353-61
PMID: 5667251
-
[The chemical mechanism of acetic acid formation in the liver].
Biochem Z. 1958;330(4):269-95
PMID: 13596371
-
Metabolism of acetoacetate in animal tissues. 1.
Biochem J. 1945;39(5):408-19
PMID: 16747930
-
Changes in activity of some enzymes involved in glucose utilization and formation in developing rat liver.
Biochem J. 1968 Jan;106(2):321-9
PMID: 4384135
-
RESPIRATORY ENZYMES IN THE HEART AND LIVER OF THE PRENATAL AND POSTNATAL RAT.
Biochem J. 1965 May;95:365-71
PMID: 14340086
-
Enzymic determination of D(-)-beta-hydroxybutyric acid and acetoacetic acid in blood.
Biochem J. 1962 Jan;82:90-6
PMID: 14007241
-
On the enzymic mechanism of acetoacetate synthesis.
Biochim Biophys Acta. 1959 Oct;35:576-7
PMID: 13834447
-
Carnitine palmitolyltransferase activity and fatty acid oxidation by livers from fetal and neonatal rats.
Can J Biochem. 1970 Mar;48(3):288-94
PMID: 4314577
-
Changes in lipid synthesis in rat liver during development.
Biochem J. 1967 Mar;102(3):952-8
PMID: 16742515
-
On the mechanism of acetoacetate synthesis by guinea pig liver fractions.
J Biol Chem. 1966 Jan 10;241(1):30-7
PMID: 5901054
-
Fatty acid utilization during development of the rat.
Biochem J. 1970 Nov;120(1):49-54
PMID: 5494228
-
Activities of enzymes of ketone-body utilization in brain and other tissues of suckling rats.
Biochem J. 1971 Jan;121(1):49-53
PMID: 5116556