In frost‐hardened spinach leaves (Spinucea oleracea L. ev. Vroeg Reuzenblad) an enhanced content of water‐soluble non‐protein sulfhydryl compounds was observed. The enhancement was due to higher levels of glutathione as well as to other non‐protein‐bound sulfhydryl compounds. In addition glutathione reductase activity was increased upon hardening. The affinity of the enzyme for oxidized glutathione was slightly lowered during hardening. The significance of glutathione accumulation during frost‐hardening is discussed. Exposure of spinach to NaCl‐stress did not affect the levels of glutathione and glutathione reductase of the leaves. In addition the kinetic properties of the enzyme remained unaltered by salinity. It is suggested that glutathione and glutathione reductase activity are not involved in adaptation of spinach to saline conditions.
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