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- W1485665613 abstract "To examine the catalytic role of sulfhydryl (SH) groups in ribulose 1,5-diphosphate (RuDP) carboxylase, the alkylation reaction of the purified spinach leaf fraction I protein was studied with a parallel determination of the enzyme activity. Before loss of enzyme activity occurred, about 4–5 SH-groups were blocked, and complete loss was associated with the blocking of 8–10 SH-groups. These values agreed with those obtained in an alkylation experiment with iodoacetamide-14C (IAA-14) with or without addition of RuDP to the enzyme protein. However, SH-groups protected by the preincubation of RuDP were released by adding bicarbonate and Mg2+ to the reaction mixture, and the final alkylation level attained was slightly higher than that observed in the non-RuDP system. This discrepancy was considered to be partly due to the structural change of the enzyme molecule in association with bicarbonate and Mg2+, which caused a change in the reactivity of SH-groups. Difficulties for assessing the direct catalytic role of SH-groups in the RuDP-carboxylase molecule were further suggested by experimental results, which showed the protective effect of carbamyl phosphate against the alkylation of SH-groups, as well as the enhancement of the proteolytic digestibility (Nagarse) of the alkylated enzyme molecule." @default.
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- W1485665613 date "1968-04-01" @default.
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- W1485665613 title "Structure and function of chloroplast proteins" @default.
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- W1485665613 doi "https://doi.org/10.1016/0003-9861(68)90644-9" @default.
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