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alpha zein/царевица
Линкът е запазен в клипборда
Страница 1 от 33 резултата
Characterization of a recombinant zein-degrading protease from Zea mays by Pichia pastoris and its effects on enzymatic hydrolysis of corn starch
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A zein-degrading protease (ZDP) from Zea mays was heterologously expressed using Pichia pastoris and its characteristics and effects on enzymatic hydrolysis of corn starch were investigated in the current study. The optimal temperature and pH for ZDP activity was 40 °C and pH 5.0, respectively. The
A defective signal peptide in a 19-kD alpha-zein protein causes the unfolded protein response and an opaque endosperm phenotype in the maize De*-B30 mutant.
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Defective endosperm* (De*)-B30 is a dominant maize (Zea mays) mutation that depresses zein synthesis in the developing endosperm. The mutant kernels have an opaque, starchy phenotype, malformed zein protein bodies, and highly increased levels of binding protein and other chaperone proteins in the
Synthesis of an unusual alpha-zein protein is correlated with the phenotypic effects of the floury2 mutation in maize.
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The soft, starchy endosperm of the maize (Zea mays L.) floury 2 mutant is associated with a reduction in zein mRNA and protein synthesis, unique protein body morphology, and enhanced levels of a 70 kDa protein, that has been shown to be the maize homolog of a chaperonin found in the endoplasmic
The nitrogen-induced recovery of alpha-zein gene expression in in vitro cultured opaque2 maize endosperms depends on the genetic background.
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The effect of nitrogen nutrition on the accumulation of seed storage proteins has been studied in vitro by cultivating on agar media maize (Zea mays L.) endosperm explants from seeds at 10 days after pollination. The experiments were performed on various genetic backgrounds bearing different opaque2
Three-dimensional structure of maize alpha-zein proteins studied by small-angle X-ray scattering.
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alpha-zeins of maize (Zea mays) that are storage proteins contain nine or ten tandem repeats comprising of about 20 amino acids. Small-angle X-ray scattering (SAXS) of alpha-zeins was measured in 70% (v/v) aqueous ethanol containing beta-mercaptoethanol or without reagent in a protein concentration
Uniparental and transgressive expression of α-zeins in maize endosperm of o2 hybrid lines.
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The α-zein gene family encodes the most abundant storage proteins of maize (Zea mays) endosperm. Members of this family are expressed in a parent-of-origin manner. To characterize this phenomenon further, we investigated the expression of a subset of α-zein polypeptides in reciprocal crosses between
Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms.
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An activity stain was used after native polyacrylamide gel electrophoresis, and at least 17 different endopeptidase activities were detected in maize (Zea mays L.) endosperm extracts prepared during the first 6 d after imbibition. The enzymes detected were classified into four groups based on their
Expression of a mutant alpha-zein creates the floury2 phenotype in transgenic maize.
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The maize floury2 mutation results in the formation of a soft, starchy endosperm with a reduced amount of prolamin (zein) proteins and twice the lysine content of the wild type. The mutation is semidominant and is associated with small, irregularly shaped protein bodies, elevated levels of a 70-kDa
Expressional profiling study revealed unique expressional patterns and dramatic expressional divergence of maize alpha-zein super gene family.
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The alpha-zein super gene family encodes the most predominant storage protein in maize (Zea mays) endosperm. In maize inbred line B73, it consists of four gene families with 41 member genes. In this study, we combined quantitative real-time PCR and random clone sequencing to successfully profile the
The Zea mays mutants opaque2 and opaque16 disclose lysine change in waxy maize as revealed by RNA-Seq.
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In maize, opaque2 (o2) and opaque16 (o16) alleles can increase lysine content, while the waxy (wx) gene can enhance the amylopectin content of grains. In our study, o2 and o16 alleles were backcrossed into waxy maize line (wxwx). The o2o2o16o16wxwx lines had amylopectin contents similar to those of
Nitrogen and hormonal responsiveness of the 22 kDa alpha-zein and b-32 genes in maize endosperm is displayed in the absence of the transcriptional regulator Opaque-2.
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The maize (Zea mays L.) b-ZIP transcriptional activator Opaque-2(O2) regulates the synthesis of major endosperm proteins. In the o2 homozygote, 22 kDa zein prolamins and the b-32 ribosome-inactivating protein are greatly reduced in level. An in vitro endosperm culture system has been studied in
Intra-Kernel Reallocation of Proteins in Maize Depends on VP1-Mediated Scutellum Development and Nutrient Assimilation.
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During maize (Zea mays) seed development, the endosperm functions as the major organ for storage of photoassimilate, serving to nourish the embryo. α-Zeins and Globulins (GLBs) predominantly accumulate in the maize endosperm and embryo, respectively. Here, we show that suppression of α-zeins by RNA
Kernel lysine content does not increase in some maize opaque2 mutants.
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The recessive mutant allele of the opaque2 gene (o2) alters the endosperm protein pattern and increases the kernel lysine content of maize (Zea mays L.). In this study, sequencing results showed that the o2 mutant was successfully introgressed into 12 elite normal maize inbred lines by marker
A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane.
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The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2
RNA interference-mediated change in protein body morphology and seed opacity through loss of different zein proteins.
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Opaque or nonvitreous phenotypes relate to the seed architecture of maize (Zea mays) and are linked to loci that control the accumulation and proper deposition of storage proteins, called zeins, into specialized organelles in the endosperm, called protein bodies. However, in the absence of null
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