Lipid metabolism and low molecular weight solute uptake in Ascaridia galli
Aggarwal, R.; Sanyal, S.N.; Khera, S.
Acta Veterinaria Hungarica 37(4): 335-347
1989
ISSN/ISBN: 0236-6290 PMID: 2638812 Document Number: 334470
The presence of important enzymes of lipid biosynthesis such as glucose-6-phosphate dehydrogenase, malate dehydrogenase and hydroxymethyl glutaryl-CoA reductase as well as an enzyme of lipid ester hydrolysis, triacylglycerol lipase were detected in A. galli. These enzymes showed subcellular distribution patterns and Michaelis-Menten kinetic characteristics comparable with those from rat liver homogenate. Studies on the uptake of labelled precursor molecules for lipid biosynthesis, glucose, acetate, and palmitate showed that the parasites can take up the isotopes readily in a time-dependent manner, showing substrate saturation kinetics, dependence upon sodium ions, and could be inhibited by the presence of the bile salts sodium cholate and sodium deoxycholate. The substrate affinity constant (Kt) and maximum apparent velocity of glucose uptake in A. galli were found to be 9.09 mM and 26.67 mM per 100 mg tissue dry weight per minute at 37 degrees C.