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1 revious biochemical characterization of dark protochlorophyllide reductase.
2 emonstrate that pc-1 was in fact a defect in protochlorophyllide reductase activity and provide the f
3 the first reproducible demonstration of dark protochlorophyllide reductase activity from purified pro
4 ted protochlorophyllide, suggesting that the protochlorophyllide reductase activity is affected by ex
7 s Mg-protoporphyrin IX methyltransferase and protochlorophyllide reductase are significantly impaired
9 e-associated biosynthetic complex containing protochlorophyllide reductase, chlorophyll synthase, ger
10 the major (36 kDa) immunodetectable form of protochlorophyllide reductase consistent with their inab
11 d sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein
12 The L protein (BchL) of the dark-operative protochlorophyllide reductase (DPOR) from Rhodobacter sp
20 eening is the result of severe repression of protochlorophyllide reductase (POR) genes by far-red lig
21 on within the fourth and fifth codons of the protochlorophyllide reductase precursor that causes a sh
24 , encoding subunits of the light-independent protochlorophyllide reductase were detected in the cotyl