Abstract
In radish (Raphanus sativus L.) cotyledons, γ-glutamyltransferase (GGT, EC 2.3.2.2) activity was detected in both fractions extracted with grinding buffer alone (low ionic strength buffer) and the same buffer supplemented with 1 M NaCl (high ionic strength buffer). The former was referred to as soluble GGT and the latter, as bound GGT. Bound GGT was not solubilized by 1% Triton X-100. The activities of both soluble and bound GGTs were inhibited by acivicin, an inhibitor of mammalian and Escherichia coli GGTs. The activity of GGT extracted with the high ionic strength buffer disappeared when protoplasts were prepared, indicating the localization of bound GGT to cell walls. These results strongly indicate the occurrence of two forms of GGTs, soluble and bound ones. The two forms of GGTs were also found in Arabidopsis thaliana, cabbage, pea, soybean, maize and rice among the eight plants tested, in addition to radish.
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