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zea mays/phosphatase
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 261 tuloksia
Alkaline phosphatase activity in lymph and serum of bile duct-ligated rats.
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To determine whether liver alkaline phosphatase (AP) reaches the circulation by crossing the space of Dissé and traversing lymphatic channels to the thoracic duct, AP was measured in lymph and serum hourly for 12 h after bile duct ligation in thoracic duct cannulated rats. AP did not rise at any
The effects of different high-fat (lard, soybean oil, corn oil or olive oil) diets supplemented with fructo-oligosaccharides on colonic alkaline phosphatase activity in rats.
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The involvement of glucose-6-phosphatase in mucilage secretion by root cap cells of Zea mays.
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In order to determine the involvement of glucose-6-phosphatase in mucilage secretion by root cap cells, we have cytochemically localized the enzyme in columella and peripheral cells of root caps of Zea mays. Glucose-6-phosphatase is associated with the plasmalemma and cell wall of columella cells.
Effects of multivalent cations on cell wall-associated Acid phosphatase activity.
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Primary cell walls, free from cytoplasmic contamination were prepared from corn (Zea mays L.) roots and potato (Solanum tuberosum) tubers. After EDTA treatment, the bound acid phosphatase activities were measured in the presence of various multivalent cations. Under the conditions of minimized
[Alkaline phosphatase of the rat small intestine--purification of the enzyme and its physiological significance].
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It has been known that feeding of high-fat diets increases in intestinal and serum alkaline phosphatase (AP) activity in rats. This phenomenon is regarded as an indirect evidence for a participation of intestinal AP (I-AP) in regard to fat absorption. This study was performed to clarify the role of
Arbuscular mycorrhizal fungal diversity, root colonization, and soil alkaline phosphatase activity in response to maize-wheat rotation and no-tillage in North China.
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Monitoring the effects of no-tillage (NT) in comparison with conventional tillage (CT) on soil microbes could improve our understanding of soil biochemical processes and thus help us to develop sound management strategies. The objective of this study was to compare the species composition and
Role of lysophosphatidylcholine in brush-border intestinal alkaline phosphatase release and restoration.
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Intestinal alkaline phosphatase (IAP) is a brush-border membrane ectoenzyme (BBM-IAP) that is released into the lumen (L-IAP) after a high-fat diet. We examined the effects of oil feeding and the addition of mixed-lipid micelles on the formation of L-IAP in oil-fed rat intestine, Caco-2 cell
Flavin-containing polyamine oxidase is a hydrogen peroxide source in the oxidative response to the protein phosphatase inhibitor cantharidin in Zea mays L.
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In this study, the specific contribution of polyamine oxidase (PAO), a hydrogen peroxide (H2O2)-producing enzyme, to the oxidative burst induced in maize mesocotyl by the phosphatase inhibitor cantharidin was examined. For this purpose, a pharmacological approach was applied using, either in vitro
Decrease in protein kinase and phosphatase activities in the liver nuclei of rats exposed to carbon tetrachloride.
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The alteration in protein kinase and phosphatase activities in the liver nuclei of rats administered carbon tetrachloride (CCl(4)) was investigated. Rats received a single oral administration of CCl(4) (1 ml/100 g body wt of 5, 10, and 25% CCl(4) in corn oil), and 5, 24, and 48 h later they were
Optimization of extraction parameters of PTP1β (protein tyrosine phosphatase 1β), inhibitory polyphenols, and anthocyanins from Zea mays L. using response surface methodology (RSM).
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BACKGROUND
Protein tyrosine phosphatase expressed in insulin-sensitive tissues (such as liver, muscle, and adipose tissue) has a key role in the regulation of insulin signaling and pathway activation, making protein tyrosine phosphatase a promising target for the treatment of type 2 diabetes
Enzymes that control the thiamine diphosphate pool in plant tissues. Properties of thiamine pyrophosphokinase and thiamine-(di)phosphate phosphatase purified from Zea mays seedlings.
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The pool of thiamine diphosphate (TDP), available for TDP-dependent enzymes involved in the major carbohydrate metabolic pathways, is controlled by two enzyme systems that act in the opposite directions. The thiamine pyrophosphokinase (TPK) activates thiamine into TDP and the numerous phosphatases
Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosophoenolpyruvate carboxylase.
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The activity and allosteric properties of plant phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) are controlled posttranslationally by specific reversible phosphorylation of a strictly conserved serine residue near the N-terminus. This up/down-regulation of PEPC is catalyzed by a dedicated and
Inorganic phosphate accumulation and phosphatase activity in the nucleus of maize embryo root cells.
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The nucleus of growing root cells Zea mays contains a high concentration of inorganic phosphate. In order to verify whether this high nuclear Pi concentration is correlated with the metabolic activity of the nucleus, the Pi has been visualized in root cells of maize embryos at the
Isolation and expression of a maize type 1 protein phosphatase.
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The dephosphorylation of phosphoproteins by protein phosphatases represents an important mechanism for regulating specific cellular processes in eukaryotic cells. The aim of the present study was to examine the structural and biochemical characteristics of a specific class of protein Ser/Thr
Effect of vanadate, molybdate, and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots.
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The effects of vanadate, molybdate, and azide on ATP phosphohydrolase (ATPase) and acid phosphatase activities of plasma membrane, mitochondrial, and soluble supernatant fractions from corn (Zea mays L. WF9 x MO17) roots were investigated. Azide (0.1-10 millimolar) was a selective inhibitor of pH
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