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alpha amylase/oryza sativa
Krækjan er vistuð á klemmuspjaldið
Bls 1 frá 106 niðurstöður
Study of growth factors, alpha-amylase and peroxidase activity in various cultivars of rice (Oryza sativa L.) under vanillic acid stress.
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The effects of Vanillic Acid (VA) on germination, seedling and adult plant of rice (Oryza sativa L.) were investigated. Four cultivars, traditional (Taroom mahalli and Taroom deilamani) and improved (Shafagh and Onda) were studied. For germination, seeds were sterilized and then placed on Petri dish
Crystal structure of α-amylase from Oryza sativa: molecular insights into enzyme activity and thermostability.
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AmyI-1 is an α-amylase from Oryza sativa (rice) and plays a crucial role in degrading starch in various tissues and at various growth stages. This enzyme is a glycoprotein with an N-glycosylated carbohydrate chain, a unique characteristic among plant α-amylases. In this study, we report the first
Possible involvement of phosphoinositide-Ca2+ signaling in the regulation of alpha-amylase expression and germination of rice seed (Oryza sativa L.).
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We have studied the effects of neomycin, a potent inhibitor of inositol phospholipid-specific phospholipase C (PLC), on the germination of rice seed and the gibberellin-induced expression of alpha-amylase in the aleurone layer and the scutellar tissues. It was shown that, in the absence of exogenous
The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase inhibitor from bran [correction of brain] of rice (Oryza sativa L.) seeds.
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A 20 kDa bifunctional inhibitor of the microbial proteinase, subtilisin, and the alpha-amylase from the larvae of the red flour beetle (Tribolium castaneum) was purified from bran of rice seeds by saline extraction, precipitation with ammonium sulphate, ion-exchange chromatography on DEAE-Cellulose
Metabolic regulation of alpha-amylase gene expression in transgenic cell cultures of rice (Oryza sativa L.).
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Expression of two genes in the alpha-amylase gene family is controlled by metabolic regulation in rice cultured cells. The levels of RAmy3D and RAmy3E mRNAs in rice cultured cells are inversely related to the concentration of sugar in the culture medium. Other genes in the rice alpha-amylase gene
The alpha-amylase genes in Oryza sativa: characterization of cDNA clones and mRNA expression during seed germination.
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Two cDNA clones, pOS103 and pOS137, were isolated which code for distinct alpha-amylase isozymes in germinating rice seeds. Sequence analysis indicated that the clones encode polypeptides of approximately 48 kDa, both of which possess a signal peptide involved in directing secretion of the protein.
Purification, crystallization and preliminary X-ray crystallographic analysis of rice bifunctional alpha-amylase/subtilisin inhibitor from Oryza sativa.
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Rice bifunctional alpha-amylase/subtilisin inhibitor (RASI) can inhibit both alpha-amylase from larvae of the red flour beetle (Tribolium castaneum) and subtilisin from Bacillus subtilis. The synthesis of RASI is up-regulated during the late milky stage in developing seeds. The 8.9 kDa
Poly(A) tail shortening of alpha-amylase mRNAs in vegetative tissues of Oryza sativa.
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The pattern of expression for the entire alpha-amylase gene family in rice vegetative tissues during the developmental growth stages has been studied. We were surprised that the size of rice alpha-amylase mRNAs in the young roots, shoots, and different tissues from adult plant was shorter by
Chromosomal localization and genomic organization of α-amylase genes in rice (Oryza sativa L.).
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Genes for α-amylase, alcohol dehydrogenase, andEm, an ABA-regulated gene expressed late in embryogenesis, were localized on rice chromosomes by the analysis of primary trisomies. The validity of the mapping approach was confirmed usingAdh-1 as a control. TheAdh-1 gene has previously been assigned to
Glutinous rice ( Oryza sativa L.) protein extract with potent α-amylase inhibitory activity
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This research screened for α-amylase inhibitory activity of twenties-five varieties Thai indigenous rice seeds. Based on specific inhibition, crude protein of var. Gai Ngaw (Gs. No. 13719) was selected for purification. The unbound proteins of the Q-Sepharose column named partially purified rice
Influence of streptomycin on alpha-amylase formation isolated endosperms & protein pattern in intact seedlings of rice Oryza sativa L.
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Expression, secretion, and processing of rice alpha-amylase in the yeast Yarrowia lipolytica.
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The gene encoding rice alpha-amylase in Oryza sativa was expressed in the yeast Yarrowia lipolytica, which is a potential host system for heterologous protein expression. For efficient secretion, the strong and inducible XPR2 promoter was used in the construction of four kinds of expression vectors
The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.
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The well-characterized secretory glycoprotein, rice (Oryza sativa) alpha-amylase isoform I-1 (AmyI-1), was localized within the plastids and proved to be involved in the degradation of starch granules in the organelles of rice cells. In addition, a large portion of transiently expressed AmyI-1 fused
Antimicrobial activity and mechanism of action of a novel cationic α-helical octadecapeptide derived from α-amylase of rice.
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AmyI-1-18, an octadecapeptide derived from α-amylase (AmyI-1) of rice (Oryza sativa L. japonica), is a novel cationic α-helical antimicrobial peptide (AMP) that contains two lysine and two arginine residues. The antimicrobial activity of AmyI-1-18 against human pathogens was quantitatively evaluated
Physicochemical and serological characterization of rice alpha-amylase isoforms and identification of their corresponding genes.
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We have identified, purified, and characterized 10 alpha-amylase isoforms from suspension-cultured rice (Oryza sativa L.) cells having different isoelectric point values. They had distinguishable optimum temperatures for enzymatic activity and molecular sizes. The results of immunoblotting indicated
Heillasta gagnagrunnur lækningajurtanna sem studdur er af vísindum
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