Metabolic control.
- M. Salter, Richard Graham Knowles, C. I. Pogson
- BiologyEssays in Biochemistry
- 1994
It is assumed that the student has acquired the knowledge taught in previous courses of the degree of Biochemistry, at first and second year's level and in the first semester of the third year.
Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
- D. Banner, A. Bloomer, S. G. Waley
- ChemistryNature
- 19 June 1975
Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheet…
Chlamydial Development Is Adversely Affected by Minor Changes in Amino Acid Supply, Blood Plasma Amino Acid Levels, and Glucose Deprivation
- Angela F. Harper, C. I. Pogson, Meirion L. Jones, J. Pearce
- BiologyInfection and Immunity
- 1 March 2000
Aberrant forms with reduced infectivity were also induced during supply of infected cell cultures with medium containing blood plasma amino acid concentrations, supporting the proposal that nutrient levels in vivo could promote abnormal chlamydial development.
Interactions of metabolism and the physiological role of insulin.
- P. J. Randle, P. Garland, C. Hales, E. Newsholme, R. Denton, C. I. Pogson
- BiologyRecent Progress in Hormone Research
- 1966
The role of tryptophan 2,3-dioxygenase in the hormonal control of tryptophan metabolism in isolated rat liver cells. Effects of glucocorticoids and experimental diabetes.
- M. Salter, C. I. Pogson
- Biology, ChemistryBiochemical Journal
- 15 July 1985
The metabolism of L-tryptophan by isolated liver cells prepared from control, adrenalectomized, glucocorticoid-treated, acute-diabetic, chronic-di diabetic and insulin-treated chronic-Diabetic rats was studied and the role of tryptophan 2,3-dioxygenase in regulating the blood tryptophile concentration is discussed with reference to its sensitivity to the above conditions.
Glycolytic and gluconeogenic enzyme activities in parenchymal and non-parenchymal cells from mouse liver.
- D. M. Crisp, C. I. Pogson
- Biology, Computer ScienceBiochemical Journal
- 1 February 1972
Parenchymal cells prepared by mechanical disruption of mouse liver with 20% polyvinyl alcohol exhibit a similar enzyme profile to those prepared enzymically, and a very substantial increase in the activity ratio of glucokinase to hexokinase over that in total liver homogenate.
The flux control coefficient of carnitine palmitoyltransferase I on palmitate beta-oxidation in rat hepatocyte cultures.
- T. Spurway, H. Sherratt, C. I. Pogson, L. Agius
- BiologyBiochemical Journal
- 1 April 1997
It is concluded that the regulatory potential of CPT I is similar at low and high physiological concentrations of palmitate, which indicates that hepatic beta-oxidation of long-chain fatty acids is controlled by the activity of carnitine palmitoyltransferase I.
The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.
- D. Trentham, C. McMurray, C. I. Pogson
- Biology, ChemistryBiochemical Journal
- 1 August 1969
Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde, suggesting that the relatively slow diol-aldehyde interconversion does not restrict the rate of glycolysis.
Dihydroxyacetone phosphate. Its structure and reactivity with -glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications.
- S. Reynolds, D. W. Yates, C. I. Pogson
- Biology, ChemistryBiochemical Journal
- 1 April 1971
Keto-dihydroxyacetone phosphate is the primary reactive species in the reactions catalysed by alpha-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase, and rate constants for these reactions have been determined.
The control of fatty acid metabolism in liver cells from fed and starved sheep.
- M. Lomax, I. Donaldson, C. I. Pogson
- Biology, MedicineBiochemical Journal
- 15 August 1983
It is suggested that propionate may control hepatic ketogenesis by acting at some point in the beta-oxidation sequence in relation to the differences in the regulation of hepatic fatty acid metabolism between sheep and rats.
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