Asparaginase is a homotetramer that catalyzes the hydrolysis of asparagine to aspartic acid and ammonia and exhibits about a 2-4% activity on glutamine and 5% on D-asparagine. Asparaginase does not occur naturally in humans but is found in bacteria, plants and many animals (e.g. guinea pigs). The enzyme has been used to reduce acrylamide, a suspected carcinogen, produced in fried starchy food products and to treat acute lymphoblastic leukemia (ALL) and some other hematopoietic neoplasms (e.g. multiple myeloma). Metabolization of asparagine prevents acrylamide formation in fried foods (Maillard reaction). The enzyme's antineoplastic effects are based on the inability of cancer cells (unlike healthy cells) to synthesize asparagine. However, the enzyme is not without some antigenicity and toxicity so it is very important to measure its activity in biological samples or monitor its activity during therapy. Sample Type: Bacteria, plants and many animals (e.g. guinea pigs) cell lysates, biol