Abstract:
:Arginase (EC 3.5.3.1) localization was studied in soybean (Glycine max L.) seedling cotyledons. Subcellular fractionation in a discontinuous Percoll gradient showed that arginase was localized in the mitochondrion. Arginine (Arg) uptake by mitochondria was demonstrated by co-sedimentation of [3H]Arg-derived label and the mitochondrial marker enzyme cytochrome c oxidase. Arginine uptake was complete in about 10 min. Since detergent but not NaCl released most label, we conclude that Arg was taken up and not bound to the organellar surface. Arginine transport was not saturable, at least up to 20 mM. Basic amino acids were the best inhibitors of Arg uptake. The uncoupler 2,4-dinitrophenol did not inhibit Arg uptake. At least 30% of L-[guanido-14C]Arg taken up by mitochondria was degraded by arginase in seedling cotyledons, while little or no degradation was detected in mitochondria from developing embryos, even though the Arg uptake level was similar in both mitochondrial preparations. These results are consistent with our previously reported pattern of arginase expression and urea accumulation during embryo development and seed germination (A. Goldraij and J.C. Polacco, 1999, Plant Physiol. 119: 297-303). The lack of Arg degradation allows developing embryos to conserve Arg, the main N-reserve amino acid utilized by germinating soybean.
journal_name
Plantajournal_title
Plantaauthors
Goldraij A,Polacco JCdoi
10.1007/s004250050056subject
Has Abstractpub_date
2000-03-01 00:00:00pages
652-8issue
4eissn
0032-0935issn
1432-2048pii
10.1007/s004250050056journal_volume
210pub_type
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