Plasma lipase properties as related to pancreatic condition.
Pantelis Arzoglou, J.-M. Lessinger, Georges Férard
Abstract
Pantelis Arzoglou, J.-M. Lessinger, Georges Férard
Abstract
We examined the sensitivity to colipase of two types of lipase (EC 3.1.1.3) activity in plasma. Results were very similar for plasma lipase corresponding to that found in cases of acute pancreatitis and for swine pancreas lipase, whereas we found some differences between "pancreatitis lipase" and lipase from healthy subjects. Gel-filtration experiments suggest that the two forms of lipase in plasma have different relative molecular masses; moreover, their avidity for antibodies against human pancreatic lipase differs. Guided by these studies, we propose optimal conditions for nephelometry of "pancreatitis" lipase.
OpenAlex reports 5 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
We examined the sensitivity to colipase of two types of lipase (EC 3.1.1.3) activity in plasma. Results were very similar for plasma lipase corresponding to that found in cases of acute pancreatitis and for swine pancreas lipase, whereas we found some differences between "pancreatitis lipase" and lipase from healthy subjects. Gel-filtration experiments suggest that the two forms of lipase in plasma have different relative molecular masses; moreover, their avidity for antibodies against human pancreatic lipase differs. Guided by these studies, we propose optimal conditions for nephelometry of "pancreatitis" lipase.
Key concepts: Lipase, Colipase, Pancreatitis, Pancreatic lipase, Pancreas, Triacylglycerol lipase, Chemistry, Avidity