Subcellular Distribution of DNA Polymerase Activity in Newborn Rat Brain and Liver

1971 ◽  
Vol 49 (12) ◽  
pp. 1285-1291 ◽  
Author(s):  
M. R. V. Murthy ◽  
A. D. Bharucha
Keyword(s):  
Enzyme Activity ◽  
Rat Brain ◽  
Dna Polymerase ◽  
Subcellular Fraction ◽  
Polymerase Activity ◽  
Particulate Material ◽  
Newborn Rat ◽  
Newborn Brain ◽  
Rat Brain And Liver ◽  
The Brain

DNA polymerase activities were determined in the cytoplasmic soluble, the nuclear soluble, and the nuclear particulate fractions of newborn rat brain and liver. The results indicate that a majority of the brain nuclear enzyme may be bound to particulate material while a majority of the liver nuclear enzyme may be free or only loosely bound. Although the subcellular distributions of DNA polymerase activity are widely different in newborn brain and liver, the enzyme activity in any given subcellular fraction is higher in liver than in brain.

DNA Polymerases of Newborn Rat Brain and Liver

1971 ◽  
Vol 49 (8) ◽  
pp. 978-986 ◽  
Author(s):  
A. D. Bharucha ◽  
M. R. V. Murthy
Keyword(s):  
Rat Brain ◽  
Specific Activity ◽  
Hydrolytic Enzymes ◽  
Polymerase Activity ◽  
Newborn Rat ◽  
Newborn Brain ◽  
Rat Brain And Liver ◽  
Mammalian Tissues ◽  
Optimum Ph ◽  
Sulfhydryl Compounds

DNA polymerase activity was found to be present in appreciable quantities in the extracts of whole tissue (TS) as well as of nuclei (NS) isolated from newborn rat brain and liver. The NS fractions of either of the two tissues exhibited a higher specific activity per unit protein than the corresponding TS fractions. The optimum pH requirements as well as the ability to support DNA synthesis over a long period indicate that the NS fractions were also comparatively less contaminated by interfering substances than the TS fractions.The reaction requirements for the incorporation of TMP residues into DNA by the NS fractions of newborn rat brain and liver and the effect of various inhibitors and hydrolytic enzymes on this reaction were also investigated. These extracts resembled preparations from other mammalian tissues in that they exhibited absolute requirements for the primer DNA, the four complimentary deoxynucleoside triphosphates, and Mg2+ ions. When three of the four deoxynucleoside triphosphates were omitted and only TTP-2-14C was added to the reaction mixture, a limited incorporation of TMP-2-14C into DNA occurred. Other investigations such as the effect of actinomycin and of sulfhydryl compounds revealed that a large part of incorporation by the TS and NS fractions of newborn brain and liver was due to the replicative DNA nucleotidyltransferase enzyme.

DNA Polymerase Activity in the Nuclei of Developing Rat Brain and Liver

1972 ◽  
Vol 50 (2) ◽  
pp. 186-189 ◽  
Author(s):  
M. R. V. Murthy ◽  
A. D. Bharucha
Keyword(s):  
Rat Brain ◽  
Dna Polymerase ◽  
Soluble Fraction ◽  
Growth Period ◽  
Polymerase Activity ◽  
Newborn Rat ◽  
A Value ◽  
Rat Brain And Liver ◽  
Dna Contents ◽  
Developing Rat

The level of DNA polymerase activity per tissue in the soluble fraction (NS) of rat brain nuclei underwent a twofold increase during the first 2 weeks after birth and then declined steeply over the next 10 weeks to a value only one-third ofthat in the newborn. In contrast to brain, the enzyme activity per liver increased continuously from birth up to 12 weeks of age (10-fold). The DNA contents of these tissues appear to be quantitatively related to the DNA polymerase activities in the respective NS fractions. These preparations did not phosphorylate thymidylate to TTP, but could convert the other three complementary deoxynucleotides to the triphosphate level. This latter activity was highest in the NS fraction of the newborn rat brain and decreased drastically with growth. In the corresponding fraction of liver, the activity remained relatively stable throughout the growth period tested.

scholarly journals Regional enzyme development in rat brain. Enzymes associated with glucose utilization

1984 ◽  
Vol 218 (1) ◽  
pp. 131-138 ◽  
Author(s):  
S F Leong ◽  
J B Clark
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Rat Brain ◽  
Brain Regions ◽  
Glycolytic Enzyme ◽  
Glycolytic Potential ◽  
Key Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Potential Enzyme Activity ◽  
The Brain

The development of key enzyme activities concerned with glucose metabolism was studied in six regions of the rat brain in animals from just before birth (-2 days) through the neonatal and suckling period until adulthood (60 days old). The brain regions studied were the cerebellum, medulla oblongata and pons, hypothalamus, striatum, mid-brain and cortex. The enzymes whose developmental patterns were investigated were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49). Hexokinase, aldolase and lactate dehydrogenase activities develop as a single cluster in all the regions studied, although the timing of this development varies from region to region. Glucose-6-phosphate dehydrogenase activity, however, declines relative to glycolytic enzyme activity as the brain matures. When the different brain regions are compared, it is clear that the medulla develops its glycolytic potential, as indicated by its potential enzyme activity, considerably earlier than the other regions (hypothalamus, striatum and mid-brain), with the cortex and cerebellar activities developing even later. This enzyme developmental sequence correlates well with the neurophylogenetic development of the brain and adds support to the hypothesis that the development of the potential for glycolysis in the brain is a necessary prerequisite for the development of neurological competence.

DNA polymerase activity in rat brain during ontogeny

1970 ◽  
Vol 23 (3) ◽  
pp. 424-432 ◽  
Author(s):  
Jo Anne Brasel ◽  
Richard A. Ehrenkranz ◽  
Myron Winick
Keyword(s):  
Rat Brain ◽  
Dna Polymerase ◽  
Polymerase Activity

DNA POLYMERASE ACTIVITY FROM THE BRAIN OF OCTOPUS VULGARIS LAM

1972 ◽  
Vol 19 (8) ◽  
pp. 1959-1965 ◽  
Author(s):  
M. Libonati ◽  
G. Liguori ◽  
A. Giuditta
Keyword(s):  
Dna Polymerase ◽  
Polymerase Activity ◽  
Octopus Vulgaris ◽  
The Brain

scholarly journals Enzyme activity and composition of myelin and subcellular fractions in the developing rat brain

1969 ◽  
Vol 115 (5) ◽  
pp. 1051-1062 ◽  
Author(s):  
N. L. Banik ◽  
A. N. Davison
Keyword(s):  
Enzyme Activity ◽  
Plasma Membrane ◽  
Rat Brain ◽  
Membrane Fraction ◽  
Subcellular Fractions ◽  
Aminopeptidase Activity ◽  
Adult Rat ◽  
Adult Rat Brain ◽  
Developing Rat ◽  
The Brain

1. Subcellular fractions and myelin were isolated from developing and adult rat brain. 2. Measurements of chemical composition and enzyme activities indicate the presence of a second myelin-like fraction mainly in the brain of developing rats. 3. This membrane fraction has a different lipid composition from myelin, but resembles myelin in its content of phosphohydrolase and aminopeptidase activity. 4. It is suggested that the second myelin-like fraction may be a submicrosomal contaminant or it may be derived from oligodendroglial plasma membrane during myelinogenesis.

scholarly journals Effect of phenylalanine metabolites on the activities of enzymes of ketone-body utilization in brain of suckling rats

1976 ◽  
Vol 160 (2) ◽  
pp. 217-222 ◽  
Author(s):  
J Benavides ◽  
C Gimenez ◽  
F Valdivieso ◽  
F Mayor
Keyword(s):  
Enzyme Activity ◽  
Mental Retardation ◽  
Rat Brain ◽  
Ketone Body ◽  
Lipid Synthesis ◽  
Developing Brain ◽  
Transferase Activity ◽  
Suckling Rats ◽  
Coa Transferase ◽  
The Brain

1. The effects of phenylalanine and its metabolites (phenylacetate, phenethylamine, phenyl-lactate, o-hydroxyphenylacetate and phenylpyruvate) on the activity of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) 3-oxo acid CoA-transferase (EC 2.8.3.5) and acetoacetyl-CoA thiolase (EC 2.3.1.9) in brain of suckling rats were investigated. 2. The 3-hydroxybutyrate dehydrogenase from the brain of suckling rats had a Km for 3-hydroxybutyrate of 1.2 mM. Phenylpyruvate, phenylacetate and o-hydroxyphenylacetate inhibited the enzyme activity with Ki values of 0.5, 1.3 and 4.7 mM respectively. 3. The suckling-rat brain 3-oxo acid CoA-transferase activity had a Km for acetoacetate of 0.665 mM and for succinyl (3-carboxypropionyl)-CoA of 0.038 mM. The enzyme was inhibited with respect to acetoacetate by phenylpyruvate (Ki equals 1.3 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). The reaction in the direction of acetoacetate was also inhibited by phenylpyruvate (Ki equals 1.6 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). 4. Phenylpyruvate inhibited with respect to acetoacetyl-CoA both the mitochondrial (Ki equals 3.2 mM) and cytoplasmic (Ki equals 5.2 mM) acetoacetyl-CoA thiolase activities. 5. The results suggest that inhibition of 3-hydroxybutyrate dehydrogenase and 3-oxo acid CoA-transferase activities may impair ketone-body utilization and hence lipid synthesis in the developing brain. This suggestion is discussed with reference to the pathogenesis of mental retardation in phenylketonuria.

scholarly journals Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by biochemical, immunochemical and kinetic studies

1985 ◽  
Vol 229 (2) ◽  
pp. 333-341 ◽  
Author(s):  
S Vora ◽  
R Oskam ◽  
G E Staal
Keyword(s):  
Skeletal Muscle ◽  
Rat Brain ◽  
Genetic Control ◽  
Kinetic Studies ◽  
Rat Brain And Liver ◽  
P Type ◽  
Regulatory Properties ◽  
The Brain ◽  
Citrate Inhibition ◽  
Allosteric Properties

In man and the rabbit, 6-phosphofructokinase (PFK, EC 2.7.1.11) exists in tetrameric isoenzymic forms composed of muscle (M or A), liver (L or B) and platelet or brain (P or C) subunits, which are under separate genetic control. In contrast, the genetic control of the rat PFK has not yet been conclusively established; it is unclear whether the P-type or C-type subunit exists in this species. To resolve this question, we investigated the enzyme from the skeletal muscle, liver and brain of rats of Wag/Rij strain. Our studies demonstrate that the rat PFK is also under the control of three structural loci and that the homotetramers M4, P4 and L4 exhibit unique chromatographic, immunological and kinetic-regulatory properties. Skeletal-muscle and brain PFKs consist of isolated M4 and P4 homotetramers respectively. Although liver PFK consists predominantly of L4 homotetramer, it also contains small amounts of PL3 and P2L2 species. All three PFKs exhibit allosteric properties: co-operativity with fructose 6-phosphate and inhibition by ATP decrease in the order P4 greater than L4 greater than M4. P4 and M4 tetramers are the most sensitive to citrate inhibition, whereas L4 tetramer is the least sensitive. More importantly, P4 and L4 isoenzymes are the most sensitive to activation by fructose 2,6-bisphosphate, whereas M4 isoenzyme is the least sensitive. These results indicate that the brain PFK in this strain of rat is a unique tetramer, P4, which also exhibits allosteric kinetics, as do the well-studied M4 and L4 isoenzymes. The reported differences in the number and nature of isoenzymes present in the rat brain and liver most probably reflect the differences in the strains studied by previous investigators. Since the nature of the rat PFK isoenzymes and nomenclatures reported by previous investigators have been now reconciled, it is proposed that, for the sake of uniformity, only well-established nomenclatures used for the rabbit or human PFK isoenzymes be used for the rat isoenzymes.

scholarly journals The occurrence of two types of deoxyribonucleic acid polymerase activity in the main classes of nuclei obtained from the brains of infant and adult rats

1974 ◽  
Vol 140 (1) ◽  
pp. 65-71 ◽  
Author(s):  
M. A. Stambolova ◽  
D. Cox ◽  
A. P. Mathias
Keyword(s):  
Rat Brain ◽  
Dna Polymerase ◽  
Gradient Centrifugation ◽  
Polymerase Activity ◽  
Synthetic Activity ◽  
Relative Distribution ◽  
Adult Rats ◽  
Different Types ◽  
Dna Template

1. The influence of exogenous or activated DNA template on the DNA polymerase activity in the different types of intact nuclei from rat brain tissue was determined. The different amounts or physical state of the DNA template did not produce significant differences in the relative distribution of the DNA polymerase activity between the separate groups of nuclei. 2. The DNA polymerase activities, fractionated by sucrose gradient centrifugation into enzyme A and enzyme B, were found to be present in the extracts of all types of rat brain nuclei. The distribution of these two activities in the ‘particulate’ and ‘soluble’ fractions of the separate groups of nuclei from 10-day-old and adult rats was studied. The findings are related to the DNA-synthetic activity in vivo of the intact nuclei and the possible biological functions of the DNA polymerase activities are discussed.

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