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Biomedical subjects

D G Walker

Publications and source records attributed to D G Walker.

At least 163 records · Page 9Linked to original sources
PubMed1968

Adaptive behaviour of some enzymes involved in glucose utilization and formation in rat liver during the weaning period.

1. The effects of premature weaning on to normal and high-glucose diets and of normal weaning on to high-protein and high-fat diets on the activities of hepatic enzymes involved in both the utilization of glucose and the formation of glucose by gluconeogenesis in rats during the weaning period were investigated. 2. The effects of weaning and high-glucose diets were, in general, to bring about increases in the activities of enzymes involved in glucose utilization and a more rapid decrease of the activities of the gluconeogenic enzymes towards normal adult values. 3. The effects of weaning on to high-fat and high-protein diets were, in general, to lower the rate of increase in activities of the enzymes involved in glucose utilization, and to prevent the decrease in activity of the gluconeogenic enzymes that occurs during normal weaning. 4. The changes in the activity of cytoplasmic phosphopyruvate carboxylase appear to be of special significance; this and other results are in keeping with current theories about the pathways and control of gluconeogenesis. 5. The activity of ATP citrate lyase appears to be particularly important in lipid formation. 6. The results are interpreted in terms of the known adaptive behaviour of these enzymes in the adult rat. The roles of enzyme development and of enzyme adaptation in the elaboration of metabolic homoeostasis in the weanling rat are discussed.

Adaptation, Physiological↗
PubMed1968

Some properties of galactokinase in developing rat liver.

1. The nature of the galactokinase present in the livers of foetal, newborn and adult rats was examined by the application of several separation procedures and by measurement of a range of kinetic parameters. 2. No evidence of enzyme heterogeneity at any stage of development was found during gel filtration on Sephadex G-100, column chromatography on DEAE-cellulose or a variety of electrophoretic procedures. 3. The K(m) values, inhibition characteristics and other kinetic parameters appear to remain constant during development. 4. Rat liver galactokinase activity does not adapt to dietary changes in either the adult or the newborn rat; hence it is unlikely that the presence of galactose in milk controls the enzymic activity profile during development. 5. On the present evidence it is concluded that only one form of galactokinase is present in rat liver and that the enzymic activity is controlled by non-dietary factors.

Age Factors↗
PubMed1968

Carbohydrate formation from various precursors in noenatal rat liver.

1. Measurements of the net synthesis of glucose plus glycogen from various precursors in slices of glycogen-depleted livers from rats at various stages of development indicated an increase in the gluconeogenic capacity after birth with l-lactate, oxaloacetate, a casein hydrolysate, l-serine, l-threonine, l-alanine and glycerol as substrates. 2. The highest rates of incorporation of (14)C-labelled precursors into glucose plus glycogen in slices of normal livers of rats of various ages were observed in such tissue preparations from neonatal animals for an amino acid mixture, l-alanine, l-serine and l-threonine. 3. The activities of rat hepatic l-serine dehydratase and l-threonine dehydratase increase rapidly after birth and show maxima about 20 days later. 4. The results provide further evidence of the increased capacity for hepatic gluconeogenesis in the neonatal period and suggest various sites of regulation of the process.

Alanine↗
PubMed1967

Further properties and possibel mechanism of action of adenosine 5'-triphosphate-D-glucose 6-phosphotransferase from rat liver.

1. Magnesium ions are the most effective bivalent ions in the glucokinase reaction. 2. The molecular weight of rat hepatic glucokinase is 48000-49000 as assessed by gel filtration on Sephadex G-100. 3. Anomalous kinetic behaviour at low glucose concentrations appears to be due to the formation during the purification procedure of fragments possessing modified catalytic properties, but is unlikely to be of physiological significance. 4. Extension of previous studies (Parry & Walker, 1966) suggests that glucokinase catalyses a reaction of the random Bi Bi type similar to that of yeast hexokinase. 5. The inhibitory effects of various thiol reagents suggest that a thiol group may be involved at or near the binding site of the acceptor molecule.

Adenosine Triphosphate↗
PubMed1967

Regulation of development of hepatic glucokinase in the neonatal rat by the diet.

1. Feeding a high-glucose diet to weanling rats showed that high hepatic glucokinase activities could be induced at 18 days of age, i.e. 2 days after development of the enzyme begins. 2. The normal development of glucokinase activity can be retarded by weaning rats on to carbohydrate-free, high-fat and high-protein diets. 3. Precocious development of the enzyme before 16 days of age cannot be induced by oral glucose administration. 4. It is concluded that the ability to synthesize glucokinase develops very rapidly and that the nature of the diet determines the normal developmental pattern.

Animals↗
PubMed1966

Purification and properties of adenosine 5'-triphospae-D-glucose 6-phosphotransferase from rat liver.

1. An 870-fold purification of glucokinase from rat liver is described which involves ammonium sulphate fractionation and the use of DEAE-Sephadex, DEAE-cellulose and polyacrylamide columns. 2. The preparation is free of any interfering enzymes and has a specific activity of 8mumoles/min./mg. of protein. 3. Glucokinase catalyses the phosphorylation of glucose, mannose and 2-deoxyglucose. 4. The enzyme is inhibited by high concentrations of glucose 6-phosphate only; ADP is an inhibitor whose effect depends on the Mg(2+) concentration. 5. The properties of glucokinase are compared briefly with those of other phosphotransferases.

Adenine Nucleotides↗
PubMed1965

The development of hepatic glucokinase in the neonatal rat.

1. Glucokinase and hexokinase activities have been determined in the livers of newborn rats and attempts made to influence in vivo the development of the glucokinase. 2. Glucokinase first appears in rat liver about 16 days after birth and adult activities are reached 10-12 days later. Evidence is presented which indicates that this represents synthesis of new protein. Hexokinase activities remain constant throughout the period of glucokinase development. 3. Both exogenous glucose and insulin are necessary for the natural development of glucokinase, for this is retarded in starved and alloxan-diabetic neonatal rats. 4. The absence of glucokinase during the first 2 weeks of extrauterine life in the rat is not due to lack of insulin. 5. Attempts to advance the time at which glucokinase first appears by infusions of glucose, insulin and chlorpropamide alone and in various combinations have resulted in marginal effects only. 6. When rats are starved for 3 days during the period of glucokinase development and then re-fed, glucokinase is more rapidly synthesized, indicating that the potential ability to synthesize glucokinase continues to develop throughout the period of starvation. 7. Some possible reasons for the comparatively late development of glucokinase are discussed.

Animals↗