Acylation of L-asparaginase with total retention of enzymatic activity

Biochimie
M B MartinsM E Cruz

Abstract

Acylation of L-asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) with complete retention of catalytic activity was achieved. Several parameters of the acylation method, based on the binding of palmitoyl residues to epsilon-NH2 groups of protein, were optimized. The correlation between the acylation degree of L-asparaginase and the retention of catalytic activity was established. For a palmitoyl chloride/protein molar ratio ranging from 50 to 900, a degree of modification of 10 to 30% and a retention of catalytic activity of 98 to 60% respectively, was observed. Hydrophobicity of 30% acylated protein was correlated with turbidity in water and octanol and was compared with the native protein. Acylated protein incorporated into liposomes, showed an increase in catalytic activity in intact form as compared to the native enzyme. By the introduction of a sequential acylation cycle, an improvement of the degree of modification with a maximal value at 50% was obtained. Total retention of catalytic activity was achieved by acylation in the presence of 8 mM L-asparagine in a reactional medium.

References

Jul 14, 1971·Journal of the American Chemical Society·M H O'Leary, G A Samberg
Sep 16, 2003·Angewandte Chemie·Rupali R Davda, James A Dumesic

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Citations

Jan 1, 1994·Cancer Chemotherapy and Pharmacology·J C JorgeM E Cruz
Sep 3, 2013·International Journal of Biological Macromolecules·Hajar AshrafiSaeid Daneshamouz
Mar 31, 1995·Annals of the New York Academy of Sciences·S RobertJ Chopineau
Mar 17, 2007·Critical Reviews in Biotechnology·Neelam VermaSneh Anand
Aug 16, 2008·Chemical Biology & Drug Design·Nina KocevarSamo Kreft
Jan 25, 2003·Biochimica Et Biophysica Acta·M M GasparM E M Cruz
Oct 3, 2006·Critical Reviews in Oncology/hematology·Umesh K NartaWamik Azmi
Jul 20, 2014·Pharmaceutical Research·M Luísa CorvoM Bárbara A F Martins

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