Time course transcriptional profiling of senescing barley leaves
نویسندگان
چکیده
منابع مشابه
Time course transcriptional profiling of senescing barley leaves
Cell senescence occurs as a part of developmental or stress-induced process. It is tightly regulated and involves a sequence of metabolic and structural alterations, eventually leading to cell death. Dark-induced leaf senescence is a useful model for studying senescence-related events. To facilitate the integration of physiological and molecular studies utilizing this model, we generated the mi...
متن کاملPartial purification and characterization of endoproteinases from senescing barley leaves.
Two major endoproteinases were purified from senescing primary barley leaves. The major enzyme (EP(1)) appeared to be a thiol proteinase and accounted for about 85% of the total proteolytic activity measured in vitro. This proteinase was purified 5,800-fold and had a molecular weight of 28,300. It was highly unstable in the absence of dithiothreitol or at a pH greater than 7.5. Leupeptin, at a ...
متن کاملProteases of Senescing Oat Leaves
Two proteases isolated from senescent oat (Avens saiva) leaves have been subjected to further study. One of these, an acid protease active at pH 4.2, is inhibited by phenylmethylsulfonyl fluoride (PMSF) but not by iodoacetamide (lAc). The other, active at pH 6.6, is inhibited by both PMSF and IAc. These results, together with previously reported evidence that mercaptoethanol stimulates the acti...
متن کاملCatabolites of chlorophyll in senescing barley leaves are localized in the vacuoles of mesophyll cells.
Senescing barley leaves accumulate a series of pink pigments with the chemical properties of catabolites derived from chlorophyll. Levels of the major component of this group of pigments were quantified by HPLC and shown to be maximal in tissues exhibiting maximal rates of chlorophyll degradation. Protoplasts were isolated from senescent leaf tissue and fractionated to yield intact vacuoles and...
متن کاملHydrolysis of Ribulose-1,5-bisphosphate Carboxylase by Endoproteinases from Senescing Barley Leaves.
The hydrolysis of (14)C-labeled ribulose-1,5-bisphosphate carboxylase (RuBPCase) by two partially purified endoproteinases from senescing barley (Hordeum vulgare v. Numar) leaves is described. The major thiol proteinase, EP(1), exhibits biphasic kinetics which appear to be caused by a region of the large subunit of RuBPCase that is highly sensitive to attack by EP(1). This proteinase further hy...
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ژورنال
عنوان ژورنال: Genomics Data
سال: 2015
ISSN: 2213-5960
DOI: 10.1016/j.gdata.2015.03.006