Purification and properties of glutathione synthetase from spinach (Spinacia oleracea) leaves |
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| Affiliation: | 1. School of Information Science and Engineering, Central South University, Changsha 410083, PR China;2. Department of Computer Science, Georgia State University, Atlanta, GA 30302, USA |
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| Abstract: | Glutathione synthetase (γ-l-glutamyl-l-cysteine:glycine ligase [ADP-forming], EC 6.3.2.3) was partially-purified (100-fold) from spinach (Spinacia oleracea) leaves and its properties determined. At least part of the enzyme activity is localized in chloroplasts. The properties of the enzyme suggest that GSH synthesis would be facilitated at the pH and Mg2+ concentration in the stroma of illuminated chloroplasts, but glutathione synthetase does not appear to be ‘light-activated’ in isolated type A chloroplasts. |
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