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Unno Keiko; Ando Ichiro; Hagima Naoko; Yokogaki Shuichi; Koike Chieko; Okada Shoji 《Plant & cell physiology》1992,33(7):963-969
The effects of deuterium (D) on Chlorella ellipsoidea C-27 wereinvestigated. Cells grown in a medium prepared with deuteriumoxide (D2O) showed pronounced delays in cell growth and division;the length of a cell cycle in medium with 100 mol% D2O was morethan 5 times longer than that in medium prepared in H2O Thedelay caused by D2O was not overcome by either indoleaceticacid or kinetin. The biological and ultrastractural characteristicsof deuterated .Chlorella (D-Chlorella) cells were examined.The responses of D-Chlorella to cell wall-digesting enzymesdid not differ from those of normal (H-Chlorella) cells. D-Chlorellacells were enlarged, and cellular components, such as proteins,nucleic acids, lipids and ATP, were present in larger quantitiesthan those in H-cells. The chloroplast of D-Chlorella was enlarged,but the levels of component photosynthetic pigments were significantlyreduced. By contrast, mitochondria of D-Chlorella were smallerthan those of H-cells. These changes in levels of cellular componentsand in the sizes of organelles seem to be unique to deuteration. (Received May 13, 1992; Accepted July 28, 1992) 相似文献
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For investigating the effect of slight modification of proteinson their higher-ordered structure, and that of chaperonin onthe functional assembly of proteins, we prepared partially deuteratedribulose 1,5-bisphosphate carboxylase (Rubisco) by cultivatingChlorella ellipsoidea in 100 mol% D2O medium. Chlorella cellsgrown in the D2O medium (D-Chlorella) contained almost the sameamount of Rubisco (D-Rubisco) as the cells grown in H2O medium(H-Chlorella) determined by Western blotting using Rubisco-specificantibody, whereas the activity of D-Rubisco determined by carbonfixation was only 28% of that of Rubisco from H-Chlorella (H-Rubisco).D-Rubisco, however, showed similar Km and pH and temperatureoptima to those of H-Rubisco as well as similar antibody bindingcapability. The enzyme activity of D-Rubisco was recovered to84% of that of H-Rubisco by the addition of GroE proteins (GroEL,chaperonin 60, and GroES, chaperonin 10), members of the chaperoninfamily produced by Escherichia coli. These data suggest thatD-Rubisco has subtle incompleteness in terms of functional assembly,a situation that is correctable by chaperonin. (Received August 8, 1994; Accepted January 9, 1995) 相似文献
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