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- W2022232191 abstract "Abstract A previous report showed that cytosolic fractions of both free-living Bradyrhizobium japonicum and soybean bacteroids exhibited high levels of pyrroline-5-car☐ylate reductase (P5CR) activity and summarized kinetic evidence for a common reductase which was distinct from that in nodule host cytosol. In the present study, a polyclonal rabbit antibody directed against P5CR in nodule host cytosol (α-[P5CR.NHC]) was prepared. Recognition of the native reductase by α-[P5CR.NHC] was shown by immunoinhibition of the catalytic activity of enzyme from nodule host cytosol: the P5CR activities in the cytosolic fractions from bacteroids and free-living rhizobia were not affected. Immunoblots showed that α-[P5CR.NHC] recognized the 30-kDa polypeptide of the purified plant reductase, as well as in nodule host cytosol. A 43-kDa polypeptide was also bound on immunoblots of Bradyrhizobium japonicum cytosol, but not of bacteroid cytosol. The 43-kDa species seems not to represent the rhizobial P5CR, but a cross-reacting antigen of currently unknown function which is deleted or modified during infection or bacteroid maturation. Antibody directed against P5CR from Escherichia coli did not recognize the reductase from nodule host cytosol, either by immunoinhibition or on immunoblots." @default.
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- W2022232191 date "1997-01-01" @default.
- W2022232191 modified "2023-09-26" @default.
- W2022232191 title "Pyrroline-5-car☐ylate reductases in soybean nodules: the enzymes in host cytosol and bacteroids are antigenically distinct" @default.
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- W2022232191 doi "https://doi.org/10.1016/s0168-9452(96)04537-2" @default.
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