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

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...

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Veröffentlicht in:	Journal of molecular microbiology and biotechnology 2015-01, Vol.25 (5), p.301-310
Hauptverfasser:	El-Sayed, Ashraf S.A., Yassin, Marwa A., Khalaf, Salwa A., El-Batrik, Mohamed, Ali, Gul Shad, Esener, Sadik
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Aspergillus - enzymology Cystathionine - metabolism Cystathionine gamma-Lyase - antagonists & inhibitors Cystathionine gamma-Lyase - chemistry Cystathionine gamma-Lyase - isolation & purification Cystathionine gamma-Lyase - pharmacokinetics Enzyme Stability Enzymes, Immobilized - chemistry Hydrogen-Ion Concentration Kinetics Polyethylene Glycols - chemistry Rabbits Research Article Substrate Specificity
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