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Pancreatic lipase activity was determined by measuring the hydrolysis of p-nitrophenolate to p-nitrophenol at 405 nm using a spectrophotometer.
Bgl.bli1 activity was determined by measuring the hydrolysis of p-nitrophenyl-β-d-glucopyranoside (pNPG) according to the method in a previous study (Shi et al. 2017).
Acid glycohydrolases were assayed by measuring the hydrolysis of PNP-glycopyranoside substrate at their optimum pH.
Specific activity was quantitatively estimated by measuring the hydrolysis of polygalacturonic acid using an equimolar quantity of AnPGI.
The activity of thrombin was determined by measuring the hydrolysis of chromogenic substrate S-2238 (H D-Phe-Pip-Arg-pNA).
Pancreatic lipase activity was determined by measuring the hydrolysis of p-NPB to p-nitrophenol using the QuantiChrom Lipase Assay Kit according to manufacturer's instructions.
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To determine if ACAP-A and ACAP-B have ArfGAP enzymatic activity, we measured the hydrolysis of GTP bound to Arf as described under "Methods".
The ratio k h S / k h, that measures the hydrolysis acceleration, is thus a natural parameter to characterize the behavior of the system.
The catalytic activities of free lipase and the lipase-NPG biocomposite were determined by measuring the initial hydrolysis rate of 4-nitrophenyl palmitate (pNPP) by lipase at 40°C, using a spectrophotometer (2100), following the increase of p-nitrophenol (pNP) concentration at 410 nm [12].
For measuring the nonspecific hydrolysis of the substrate, an inhibitor-treated cell lysate control was included.
SAMHD1 activation by GTP, acyclovir-TP, and ganciclovir-TP was also analyzed by measuring the TTP hydrolysis rate as a function of the activator concentration (Fig. 5C).
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