-transparent.png){kind=logo}
Pancreatic lipase and phospholipase A2 have been shown by the monomolecular film technique to be progressively inactivated when adsorbed at the interface of their respective substrates. This inactivation is faster for lipase than for phospholipase. It is also enhanced by low film pressures and film transfer. The use of radioactive phospholipase and lipase samples offered the possibility to measure the amount of enzyme adsorbed at a monomolecular film with a reasonable accuracy. This adsorption was found to be relatively slow under the conditions of the assays. The main conclusion drawn from these data is that the enzyme kinetics in presence of a substrate film, and probably also under bulk conditions, is controlled by an adsorption flux responsible for an initial lag period and an inactivation flux tending to decrease the reaction rate. The kinetics are linear only when both fluxes equilibrate.
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
June 1984,
Shigaku = Odontology; journal of Nihon Dental College,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
December 2022,
Biotechnology advances,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
January 1971,
Acta pharmacologica et toxicologica,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
February 1972,
Kekkaku : [Tuberculosis],
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
October 1920,
The Journal of experimental medicine,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
April 1973,
Strahlentherapie,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
June 1961,
The Journal of biological chemistry,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
January 1986,
Monographs on atherosclerosis,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
June 2023,
Journal of cellular biochemistry,
J Rietsch, and
F Pattus, and
P Desnuelle, and
R Verger
January 1969,
Transactions of the Royal Society of Tropical Medicine and Hygiene,
