How do you measure asparaginase activity?
Asparaginase activity is measured in patient serum samples by a series of coupled enzymatic reactions occurring in a 96-well UV transparent microplate. In the first reaction, L-asparaginase in the patient sample catalyzes the hydrolysis of L-asparagine to L-aspartate (Figure 1A).
What class of enzyme is asparaginase?
Asparaginase is a bacterial enzyme that reduces the availability of asparagine, an amino acid that is necessary for the growth of some tumor cells.
What is the substrate of asparaginase?
Asparaginase reacts with the substrate (l-asparagine) to form the enzyme–substrate complex and generate the product (ammonia); then the presence of ammonia is determined by the addition of the aquarium test kit solutions that shows a change of color (orange to green).
What is the function of asparaginase?
All cells need a substance called asparagine to make proteins and create new cells. Asparaginase is an enzyme that breaks down asparagine. Unlike normal cells, ALL cells are unable to make their own asparagine. So asparaginase stops the cancer cells from dividing and growing.
Is asparaginase a hydrolase?
l-Asparaginase (a hydrolase converting l-asparagine to l-aspartic acid) was the first enzyme to be used in clinical practice as an anticancer agent after its approval in 1978 as a component of a treatment protocol for childhood acute lymphoblastic leukemia.
What is the mechanism of action of asparaginase?
Asparaginase works by breaking down the amino acid known as asparagine without which the cancer cells cannot make protein.
What is asparaginase used for?
Asparaginase erwinia chrysanthemi is used with other chemotherapy medications to treat acute lymphocytic leukemia (ALL; a type of cancer of the white blood cells).
What is asparaginase and how does it work?
Asparaginase is an enzyme that breaks down asparagine. Unlike normal cells, ALL cells are unable to make their own asparagine. So asparaginase stops the cancer cells from dividing and growing.
How do you make asparaginase?
L-asparaginase is produced from a variety of microbial sources including fungi, yeast, bacteria and actinomycetes by the process of submerged fermentation8. Currently, L-asparaginases derived from two bacterial sources, Erwinia chrysanthemi and E. coli, are in clinical use for the treatment of ALL9.