Objectivel-Asparaginase (ASNase) is an enzyme used in the treatment of acute lymphoblastic leukemia (ALL). As the therapeutic ASNases has bacterial origin, severe side effects are associated with its use, among them hypersensitivity and inactivation of the enzyme. In this context, the objective of this work was to produce a recombinant ASNase of bacterial origin in human cells in order to determine the presence and consequences of potential post-translational modifications on the enzyme.ResultsRecombinant ASNase was expressed in human cells with a molecular weight of 60 kDa, larger than in Escherichia coli, which is 35 kDa. N-glycosylation analysis demonstrated that the increased molecular weight resulted from the addition of glycans to the protein by mammalian cells. The glycosylated ASNase presented in vitro activity at physiological pH and temperature. Given that glycosylation can act to reduce antigenicity by masking protein epitopes, our data may contribute to the development of an alternative ASNase in the treatment of ALL in patients who demonstrate side effects to currently marketed enzymes.
The excessive demand for publications results in high plagiarism and duplicate numbers by scientists who take over existing texts into new publications. In addition to serious ethical problems, this practice hinders the generation of original material. In order to reduce the problem, softwares such as eTBLAST are being used to detect plagiarism and repeated papers. Despite the persistence of fraudsters, these tools have helped to reduce these problems; however, the ideal solution would be the basic ethical establishment principles. Therefore, plagiarism has always been a foible that could lead to fraudulent and dishonorable development of science.
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