Biologisches Institut II der Universität, Schänzlestrasse 1, D-7800, Freiburg, Germany.
Planta. 1983 Jul;157(4):381-3. doi: 10.1007/BF00397412.
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.
研究了光诱导下大麦中 NADPH:原叶绿素氧化还原酶迅速减少过程中的蛋白水解作用。在黄化大麦幼苗的质体制剂中存在一种最适 pH 值为 4.5 的蛋白水解活性。未检测到其他蛋白水解活性。蛋白水解的最适温度为 50°C,以血红蛋白作为底物时,测定的比活度最高。与之前的提议相反,在光诱导黄化质体转化为叶绿体的过程中,没有发现这种蛋白酶特异性参与的证据。