In situ kinetic parameters of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase in different areas of the rat liver acinus

1989 ◽  
Vol 21 (9-10) ◽  
pp. 585-594 ◽  
Author(s):  
Geertruida N. Jonges ◽  
Cornelis J. F. Van Noorden
Keyword(s):  
Kinetic Parameters ◽  
Rat Liver ◽  
Phosphogluconate Dehydrogenase ◽  
Liver Acinus ◽  
Glucose 6 Phosphate Dehydrogenase

Heterogeneity of kinetic parameters of enzymes in situ in rat liver lobules

1995 ◽  
Vol 103 (2) ◽  
pp. 93-101 ◽  
Author(s):  
C. J. F. Noorden ◽  
G. N. Jonges
Keyword(s):  
Kinetic Parameters ◽  
Rat Liver

scholarly journals Changes in activity of some enzymes involved in glucose utilization and formation in developing rat liver

1968 ◽  
Vol 106 (2) ◽  
pp. 321-329 ◽  
Author(s):  
R. G. Vernon ◽  
D G Walker
Keyword(s):  
Malate Dehydrogenase ◽  
Rat Liver ◽  
Postnatal Period ◽  
Supernatant Fraction ◽  
Atp Citrate Lyase ◽  
Carboxylase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Citrate Lyase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Developing Rat

1. The activities of some enzymes involved in both the utilization of glucose (pyruvate kinase, ATP citrate lyase, NADP-specific malate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and NADP-specific isocitrate dehydrogenase, all present in the supernatant fraction of liver homogenates) and the formation of glucose by gluconeogenesis (glucose 6-phosphatase in the whole homogenate and fructose 1,6-diphosphatase, phosphopyruvate carboxylase, NAD-specific malate dehydrogenase and fumarase in the supernatant fraction) have been determined in rat liver around birth and in the postnatal period until the end of weaning. 2. The activities of those enzymes involved in the conversion of glucose into lipid are low during the neonatal period and increase with weaning. NADP-specific malate dehydrogenase first appears and develops at the beginning of the weaning period. 3. The marked increase in cytoplasmic phosphopyruvate carboxylase activity at birth is probably the major factor initiating gluconeogenesis at that time. 4. The results are discussed against the known changes in dietary supplies and the known metabolic patterns during the period of development.

scholarly journals In situ kinetic parameters of glucose-6-phosphatase in the rat liver lobulus.

1992 ◽  
Vol 267 (7) ◽  
pp. 4878-4881
Author(s):  
G.N. Jonges ◽  
C.J. Van Noorden ◽  
W.H. Lamers
Keyword(s):  
Kinetic Parameters ◽  
Rat Liver

The effects of pregnancy, lactation and involution on the metabolism of glucose and acetate by rat liver tissue

1973 ◽  
Vol 40 (3) ◽  
pp. 339-351 ◽  
Author(s):  
R. W. Smith
Keyword(s):  
Fatty Acids ◽  
Rat Liver ◽  
Milk Fat ◽  
Late Pregnancy ◽  
Acetyl Coa Carboxylase ◽  
Atp Citrate Lyase ◽  
Phosphogluconate Dehydrogenase ◽  
Citrate Lyase ◽  
Pregnancy And Lactation ◽  
Glucose 6 Phosphate Dehydrogenase

SummaryThe incorporation of 14C from [1-14C] and [6-14C]glucose and [2-14C]acetate into CO2 and fatty acids by rat liver slices was measured at intervals during pregnancy, lactation and involution.During late pregnancy, the rates of oxidation of the C-1 and C-6 atoms of glucose were respectively 65 and 40 % higher than those for unmated animals. These increases were maintained during lactation, but the highest values were observed 3 days after weaning. Pregnancy and lactation had little effect on the oxidation of [2-14C]acetate.The incorporation of14C from all 3 labelled substrates into fatty acids was increased by a factor of 3–4 during late pregnancy. There were further increases during lactation, and 3 days after weaning the values were as much as 10 times as high as those for unmated animals.The incorporation of both [14C]glucose and [14C]acetate into cholesterol was increased by a factor of 6–7 during lactation.The activities of the enzymes glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, ATP citrate lyase and acetyl-CoA carboxylase were also increased during lactation and involution.The similarity between the changes summarized above and those brought about by changes in the pattern of food intake is discussed, and the idea that fatty acids synthesized from non-lipid precursors in the liver may make some contribution to the formation of milk fat is also considered.

scholarly journals Complementary distribution of carbamoylphosphate synthetase (ammonia) and glutamine synthetase in rat liver acinus is regulated at a pretranslational level.

1988 ◽  
Vol 36 (7) ◽  
pp. 751-755 ◽  
Author(s):  
A F Moorman ◽  
P A de Boer ◽  
W J Geerts ◽  
L van den Zande ◽  
W H Lamers ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Rat Liver ◽  
Cdna Probe ◽  
Proximal Part ◽  
Adult Rat ◽  
Liver Acinus ◽  
Complementary Distribution ◽  
Carbamoylphosphate Synthetase ◽  
Silver Grains

We studied the distribution of the mRNAs for carbamoylphosphate synthetase (ammonia) and glutamine synthetase in frozen sections of adult rat liver by in situ hybridization to [35S]-labeled cDNA probes. The density of silver grains resulting from hybridization to the labeled cDNA probe for carbamoylphosphate synthetase is highest around the portal venules, decreases towards the central venule, and is virtually absent from an area two to three cells wide that lines the central venules in which mRNA for glutamine synthetase is predominantly localized. Therefore, both mRNAs show the same complementary distribution within the liver acinus that was found for the proteins they encode, demonstrating that compartmentalization of the expression of these enzymes is controlled at a pretranslational level. In addition, we found that carbamoylphosphate synthetase mRNA is present mainly in the epithelium of the crypts of the proximal part of the small intestine, whereas carbamoylphosphate synthetase protein is present in the epithelium of both crypts and villi.

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