Biochemical and Pharmacokinetic Properties of PEGylated Cystathionine γ-Lyase from Aspergillus carneus KF723837

Journal of Molecular Microbiology and Biotechnology
Ashraf S El-SayedSadik Esener

Abstract

Cystathionine γ-lyase (CGL) was purified to its electrophoretic homogeneity from Aspergillus carneus by various chromatographic approaches. The purified enzyme has four identical subunits of 52 kDa based on SDS and native PAGE analyses. To improve its structural stability, purified CGL was modified by covalent binding to polyethylene glycol moieties. The specific activity of free-CGL and PEG-CGL was 59.71 and 48.71 U/mg, respectively, with a PEGylation yield of 81.5 and 70.7% modification of surface ε-amino groups. Free- and modified CGL have the same pattern of pH stability (8.0-9.0). At 50 °C, the thermal stability [half-life time (T1/2)] of PEG-CGL was increased by 40% in comparison to free-CGL. The activity of CGL was completely inhibited by hydroxylamine and Hg(+2), with no effect by EDTA. Free-CGL (0.04 mM(-1)s(-1)) and PEG-CGL (0.03 mM(-1)s(-1)) have a similar catalytic efficiency to L-cystathionine as a substrate. The inhibition constant values of propargylglycine were 0.31 and 0.52 µM for the free- and PEG-CGL, respectively. By in vitro proteolysis, PEG-CGL retains >50% of its initial activity compared to <10% of the free-CGL for acid protease for 30 min. From in vivo pharmacokinetics in New Zealand white rabbits, the ...Continue Reading

Citations

Aug 1, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ashraf S A El-SayedMahmoud Z Sitohy
Jul 8, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ashraf S A El-SayedBasel Sitohy
Oct 8, 2020·Heliyon·Manal T El Sayed, Ashraf S A El-Sayed

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