L-asparaginase (L-ASNase) (EC 3.5.1.1) is an important enzyme for the treatment of acute lymphoblastic leukaemia. Currently, the enzyme is obtained from bacteria, Escherichia coli and Erwinia chrysanthemi. The bacterial enzymes family is subdivided in type I and type II; nevertheless, only type II have been employed in therapeutic proceedings. However, bacterial enzymes are susceptible to induc...

l-asparaginase has lots of medical and industrial applications. ever since l-asparaginase anti-tumor activity was first demonstrated, its production using microbial systems has attracted considerable attention owing to their cost-effective and eco-friendly nature. the aim of this study is to obtain l-asparaginase producing bacteria and determining the enzyme activity. samples were picked up fro...

BACKGROUND In the recent years, there has been an increasing interest in secretory production of recombinant proteins, due to its various advantages compared with intracellular expression. Signal peptides play a critical role in prosperous secretion of recombinant proteins. Accordingly, different signal peptides have been assessed for their ability to produce secretory proteins by trial-and-err...

The enzymatic mechanism of asparaginase action has been explored using the acyl acceptor, hydroxylamine. Asparaginase catalyzed the synthesis of the hydroxamate from asparagine and more slowly from aspartic acid. P-Aspartohydroxamate was also a substrate for asparaginase. These reactions have rates which are linearly dependent on the concentration of the enzyme and can therefore be used as conv...

Acute lymphoblastic leukemia (ALL) is a heterogeneous disease, and the long-term survival varies with different ages. We performed a retrospective analysis of 122 newly diagnosed adults with standard-risk ALL treated with Escherichia coli asparaginase (E. coli-asparaginase, n = 50) and polyethylene glycol-conjugated asparaginase (PEG-asparaginase, n = 72). No treatment-related mortality (TRM) o...

In vivo metabolism of lysine and arginine is markedly inhibited (p < 0.025) in P1798 lymphosarcoma within 1 hr after intraperitoneal injection of 1 unit of Escherichia coli L-asparaginase II. Two hr after treatment, there is substan tial inhibition of thymidine transport but no effect on incorporation of thymidine. None of these effects were observed in the L-asparaginase-resistant subline of t...

Asparaginase was extracted from plant parts of Pisum sativum subspp. Jof collected from a field crop. Asparaginase activity was detected in seeds, stems and leaves extracts. Enzyme activity was higher in seeds extracts (30.0 U/ml) compared with leaves extracts (26.4 U/ml) and stems extracts (16.1 U/ml), respectively. Optimum conditions for the activity of crude asparaginase extracted from plant...

Background L-asparaginase II (asnB), a periplasmic protein commercially extracted from E coli and Erwinia, is often used to treat acute lymphoblastic leukemia. an enzyme that converts L-asparagine aspartic acid ammonia. Cancer cells are dependent on asparagine other sources for growth, when these deprived of by the action enzyme, cancer selectively die. Objective Questions remain as whether asn...

l-asparaginase is a candidate enzyme for anti-neoplastic agent againstacute lymphoblasticleukemia and also extensively use in the food industry for prevention of acrylamide formation. l-asparaginase is widely distributed among microorganisms. in this study, marine bacteria were isolated from persian gulf and screened for l-asparaginase activity. production of l-asparaginase was carried out by u...