Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thioredoxin reductase was unfolded in 2 M guanidine hydrochloride as revealed by fluorescence and CD spectroscopy. Spontaneous refolding of denatured species resulted in low recovery of 10% catalytic activity after 4 h incubation at 25 degrees C. Addition of groEL or protein disulfide isomerase to the renaturation buffer accelerated the rate of recovery of catalytic activity to a level of 35 and 15%, respectively. Fluorescence spectroscopy has been used to investigate the interaction of groEL and protein disulfide isomerase with denatured thioredoxin reductase tagged with a fluorescent probe. The fluorescence emitted by the denatured protein was quenched upon binding to either groEL or protein disulfide isomerase. It is suggested that encapsulation of the protein substrate by the chaperone plays an important role in the process of folding by facilitating the formation of correctly folded species.
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PMID:Refolding of thioredoxin reductase assisted by groEL and PDI. 1008 48

Our previous study revealed a cytokinin-related retardation of post-harvest floret yellowing in transgenic broccoli (Brassica oleracea var. italica) that harbored the bacterial isopentenyltransferase (ipt) gene. We aimed to investigate the underlining mechanism of this delayed post-harvest senescence. We used 2D electrophoresis and liquid chromatography-electrospray ionization-mass spectrometry/mass spectrometry for a proteomics analysis of heads of ipt-transgenic and non-transgenic inbred lines of broccoli at harvest and after four days post-harvest storage. At harvest, we found an accumulation of stress-responsive proteins involved in maintenance of protein folding (putative protein disulfide isomerase, peptidyl-prolyl cis-trans isomerase and chaperonins), scavenging of reactive oxygen species (Mn superoxide dismutase), and stress protection [myrosinase-binding protein, jasmonate inducible protein, dynamin-like protein, NADH dehydrogenase (ubiquinone) Fe-S protein 1 and stress-inducible tetratricopeptide repeat-containing protein]. After four days' post-harvest storage of non-transgenic broccoli florets, the levels of proteins involved in protein folding and carbon fixation were decreased, which indicates cellular degradation and a change in metabolism toward senescence. In addition, staining for antioxidant enzyme activity of non-transgenic plants after post-harvest storage revealed a marked decrease in activity of Fe-superoxide dismutase and ascorbate peroxidase. Thus, the accumulation of stress-responsive proteins and antioxidant enzyme activity in ipt-transgenic broccoli are most likely associated with retardation of post-harvest senescence.
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PMID:Proteomic analysis of stress-related proteins in transgenic broccoli harboring a gene for cytokinin production during postharvest senescence. 2176 40