Abstract
The role of proteolysis during the light-induced rapid decrease of the NADPH: protochlorophyllide oxidoreductase in barley was studied. A proteolytic activity with a pH optimum of 4.5 was present in a plastid preparation of etiolated barley seedlings. No other proteolytic activity could be detected. The temperature optimum for the proteolysis was 50°C, and the highest specific activity was measured with hemoglobin as the substrate. In contrast to previous proposals, no evidence for the specific involvement of this protease was found during the light-induced transformation of etioplasts to chloroplasts.