Pantelis Arzoglou

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Three different techniques of lipase (EC determination (titrimetry, nephelometry, and enzyme immunoassay) were used to investigate an interesting effect of ionic strength on enzyme activity. Both activation in the presence of NaCl (140 mmol/L) and strong immunoinhibition were observed for lipase from plasma of subjects with acute pancreatitis.(More)
A novel approach for the determination of pancreatic lipase (EC activity by a spectrophotometric method is described. Enzyme activity is measured in the presence of 1 mmol/l triolein, a concentration much higher than usually employed in turbidimetry. The primary reaction medium is optimized as regards bile salt and colipase concentrations. The(More)
A novel approach is described for the quantitation of the parameters involved in lipolytic activity. The activity of lipase purified from human pancreatic juice against an oil-water emulsion depends on the degree of emulsification, the type of emulsifier used, the type and the concentration of bile salt, the concentration of colipase and, finally, on the(More)
Serum lipase levels are much greater in cases of chronic alcoholics (without any marked symptom of pancreatitis) than in healthy subjects. In fact, about 43 p. cent of the studied samples from alcoholics exhibit a lipase activity above the reference interval (0-160 U/l). On the other hand, the lipase activity present in the serum of alcoholics exhibits(More)
The comparative diagnostic value of plasma lipase and amylase levels was evaluated in 90 patients with various symptoms of pancreatic disease. Comparison with healthy subjects showed that the lipase assay was more sensitive than the amylase assay in patients with acute pancreatitis or post-traumatic pancreatic injury, but not in patients with chronic(More)
Evidence is presented of the existence of at least two forms of lipase (A and B) in homogenized rabbit pancreas. These forms are separated by means of gel filtration and anion-exchange chromatography. Both forms are colipase-dependent, but lipase A is activated to a significant extent by 140 mmol/l NaCl even in the absence of the protein cofactor. Lipase A(More)
luman pancreatic lipase assays are usually performed in ie presence of either emulsified triglycerides or diglycerles within the limits of their solubility. Two reactions are atalyzed in the presence of triglycerides: hydrolysis of iglycerides to diglycerides, and diglycerides to monolycerides. The contribution of each reaction to the final sult was(More)
Lipolysis is regulated by the presence of amphiphilic compounds such as bile salts and lecithin, which are adsorbed at the triglyceride-water interface and therefore influence the approach of water-soluble pancreatic lipase to its insoluble substrate (emulsified triglycerides). The partition of bile salts between the lipid and the aqueous phase is of prime(More)
Factor VIIa (FVIIa) and thrombin generation occur in patients suffering an acute coronary event. We studied the effect of treatment with enoxaparin on FVIIa and prothrombin activation in patients with unstable angina. Anti-Xa activity, FVIIa, FVII coagulant activity (FVII:C) and FVII antigen (FVII:Ag), free tissue factor pathway inhibitor (TFPI), and(More)
Following the selection of the most appropriate method for emulsification and the optimization of the reaction medium, interlaboratory studies were conducted to check the effect of preparing substrates and measuring the catalytic concentration of lipase at different sites as well as the effect of transport on emulsion. The determinations of lipase activity(More)