scholarly journals Time Course of Starch Biosynthesis Enzymes Activity and Root Tuber Starch of Four Cassava Cultivars

2017 ◽  
Vol 5 (1) ◽  
pp. 103
Author(s):  
Huifang Huang ◽  
Yanchun Luo ◽  
Qiang Huang ◽  
Yinong Tian ◽  
Huimin Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Time Course ◽  
Starch Content ◽  
Growth Period ◽  
Sucrose Phosphate Synthase ◽  
Soluble Starch ◽  
Root Tuber ◽  
Related Enzyme ◽  
Total Starch

To understand the accumulation rule of cassava root tuber starch, the amylose, amylopectin and total starch content of fresh root tuber, the enzyme activities of sucrose synthase (SuS, EC 2.4.1.13) and sucrose phosphate synthase (SPS, EC 2.4.1.14) of leaves, the enzyme activities of ADP-glucose pyrophosphorylase (AGPase, EC 2.7.7.27), soluble starch synthase (SSS, EC 2.4.1.21) and starch branching enzyme (SBE, EC. 2.4.1.18) of tubers were assessed by using cultivars SC201, SC205, GR891 and GR911 leaves and root tubers during their growth period, respectively. The results as follows: the enzyme activity of leaf SPS and the synthesis direction of SuS showed the highest at August, 2010, however the enzyme activity of the decomposing direction of SuS formed parabolic curve; the enzyme activity of tuber AGPase showed an increased then decreased single peak curve, the enzyme activity of tuber SSS oscillating decreased, while the enzyme activity of SBE was relatively stable; the amylose, amylopectin and total starch contents of fresh cassava tuber were all gradually increased along with the growth period. This research would enrich our knowledge of the time course of amylose, amylopectin and total starch contents of fresh cassava tuber, and above related enzyme activities.

scholarly journals Rat uterine microbiochemistry: metabolic enzyme activities stimulated by 17-beta-estradiol are localized in epithelial cells.

1987 ◽  
Vol 35 (6) ◽  
pp. 657-662 ◽  
Author(s):  
J P Holt ◽  
E Rhe
Keyword(s):  
Enzyme Activity ◽  
Smooth Muscle ◽  
Epithelial Cells ◽  
Dose Response ◽  
Enzyme Activities ◽  
Time Course ◽  
Citrate Synthase ◽  
Ovariectomized Rats ◽  
Similar Response ◽  
Estradiol Treatment

Lactate dehydrogenase (LDH; EC 1.1.1.27), citrate synthase (CS; EC 4.1.3.7), and beta-hydroxyacyl-CoA-dehydrogenase (beta-OH-acyl-CoA-DH; EC 1.1.1.35) activities were determined in each of the three major cell types of rat uterus, i.e., epithelial, stromal, and smooth muscle, using quantitative microanalytical techniques. Adult ovariectomized rats were treated with 17-beta-estradiol to determine the time course and dose response (0.025-50 micrograms/300-g rat) effect of estrogen on enzyme activity of each type of uterine cell. The use of "oil well" and enzyme-cycling microtechniques to determine the time course and the dose responses of enzyme activity changes required microassays involving 1595 microdissected single cell specimens. Estradiol treatment increased epithelial LDH, CS and beta-OH-acyl-CoA-DH activity but had no effect on these enzymes in the stroma or in smooth muscle cells. The estradiol-stimulated peak enzyme activities on Day 4 in the intervention group are compared with those in the ovariectomized rat controls as follows: LDH, 44.5 +/- 3.5 vs 22.3 +/- 3.9; CS, 3.5 +/- 0.2 vs 1.5 +/- 0.6; beta-OH-acyl-CoA-H, 3.5 +/- 0.32 vs 2.2 +/- 0.2 (mean +/- standard deviation; mol/kg/hr). Stromal cell activities (LDH, 7.4 +/- 1.0; CS, 1.2 +/- 0.2; beta-OH-acyl-CoA-DH, 0.9 +/- 0.1) were significantly lower than epithelial cell levels and were similar to smooth muscle levels. Therefore, even in the ovariectomized animal epithelial cells have markedly higher metabolic activity compared with adjacent cells. The enzyme activities are expressed as moles of substrate reacting per kilogram of dry weight per hour. All three enzymes exhibited a 17-beta-estradiol-induced dose response between 0.025-0.15 micrograms/300-g rat. The three enzymes studied all had similar response patterns to estrogen. The effect of estradiol was restricted to epithelial cells, with enzyme activities increasing to maximal levels after approximately 96 hr of hormone treatment. This study therefore not only confirms the specific and differential metabolic responses of uterine cells to estradiol treatment, but clearly demonstrates that marked metabolic differences exist between epithelial cells and stromal or smooth muscle uterine cells.

scholarly journals Changes in Starch Content and Related Enzyme Activities during the Growth of Germinating Soybeans

1986 ◽  
Vol 50 (12) ◽  
pp. 3195-3196
Author(s):  
Mikio Suda ◽  
Toshiyuki Watanabe ◽  
Mikihiko Kobayashi ◽  
Kazuo Matsuda
Keyword(s):  
Enzyme Activities ◽  
Starch Content ◽  
Related Enzyme

scholarly journals Changes in starch content and related enzyme activities during the growth of germinating soybeans.

1986 ◽  
Vol 50 (12) ◽  
pp. 3195-3196 ◽  
Author(s):  
Mikio SUDA ◽  
Toshiyuki WATANABE ◽  
Mikihiko KOBAYASHI ◽  
Kazuo MATSUDA
Keyword(s):  
Enzyme Activities ◽  
Starch Content ◽  
Related Enzyme

scholarly journals Mitochondrial proliferation in the permanent vs. temporary cold: enzyme activities and mRNA levels in Antarctic and temperate zoarcid fish

2003 ◽  
Vol 285 (6) ◽  
pp. R1410-R1420 ◽  
Author(s):  
M. Lucassen ◽  
A. Schmidt ◽  
L. G. Eckerle ◽  
H.-O. Pörtner
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Time Course ◽  
Citrate Synthase ◽  
Expression Patterns ◽  
Thermal Adaptation ◽  
Lipid Synthesis ◽  
Mrna Levels ◽  
Transcript Levels ◽  
Cold Adapted

Adjustments in mitochondrial properties and capacities are crucial in acclimatization to seasonal cold and in evolutionary cold adaptation of marine ectotherms. Although long-term compensatory increments in aerobic capacity of fish tissues have frequently been described in response to cold, much less is known about transitional phases and gene expression patterns involved. We investigated the time course of adjustment to acute cold in liver of eurythermal eelpout Zoarces viviparus. Whereas citrate synthase (CS) activity rose progressively in liver, cytochrome c oxidase (COX) activity was not altered during cold acclimation. Species-specific RNA probes were used to determine mRNA levels. CS mRNA (nuclear encoded) displayed a delayed, transient increase in response to cold, such that transcript levels did not parallel the change in enzyme activity. The enzyme activities and mRNA levels in the confamilial Antarctic Pachycara brachycephalum indicate cold compensation of CS activity in this cold-adapted species. The ratio of CS and COX activities was elevated in acclimation and adaptation to cold, indicating enhanced citrate synthesis over respiratory chain capacities in cold-adapted liver mitochondria. This may support enhanced lipid synthesis typically found in cold. The ratio of enzyme activity and transcript levels differed largely between Z. viviparus populations from the Baltic and North Seas, indicating the influence of unidentified parameters other than temperature. Transcript levels may not be tightly correlated with enzyme activities during thermal adaptation and thereafter. The time course of the acclimation process indicates that regulation at the translational and posttranslational levels predominates in adjustment to moderate thermal challenges.

Effects of the Herbicide Pretilachlor and the Safener Fenclorim on Glutathione Content and Glutathione-Dependent Enzyme Activity of Rice

1991 ◽  
Vol 46 (9-10) ◽  
pp. 861-865 ◽  
Author(s):  
Seong Han ◽  
Kriton K. Hatzios
Keyword(s):  
Enzyme Activity ◽  
Time Course ◽  
Reduced Glutathione ◽  
Oryza Sativa L ◽  
Rice Seedlings ◽  
Glutathione S Transferase ◽  
Simultaneous Application ◽  
Related Enzyme ◽  
Time Course Study ◽  
Gst Activity

Abstract The influence of individual or combined treatments of the chloroacetanilide herbicide preti­lachlor and the safener fenclorim on glutathione content and the activity of glutathione reduc­tase (GR, EC 1.6.4.2) and glutathione-S-transferase (GST, EC 2.5.1.18) of rice (Oryza sativa L., var. Lamont) was investigated in a time-course study including 0, 12, 24, 48, and 72 h peri­ods after treatment. Pretilachlor applied alone at 2 μM did not influence the levels of total or reduced glutathione of germinating rice seedlings. Fenclorim applied alone at 20 μM increased significantly the levels of total and reduced glutathione of rice seedlings at 12, 24, and 72 h after treatment. The combination of pretilachlor and fenclorim increased the levels of total and reduced glutathione of rice at all time periods. GR activity extracted from pretilachlor-treated rice seedlings was significantly lower than that extracted from untreated rice seedlings. Pretreatment of rice seedlings with the safener fenclorim increased GR activity at 12 and 24 h, but not at 48 and 72 h after treatment. GR activity extracted from rice seedlings treated with the combination of pretilachlor and fenclorim was significantly higher than that of untreated controls at 12, 24, and 48 h after treatment. Pretreatment of rice seedlings with pretilachlor reduced the activity of GST which catalyzes the conjugation of this herbicide with reduced glutathione at time intervals greater than 24 h. Pretreatment with fenclorim did not have any effect on GST activity of rice seedlings. Pretreatment with the combination of pretilachlor and fenclorim increased GST activity of rice seedlings at the 48 and 72 h periods. These results suggest that a simultaneous application of pretilachlor and fenclorim is critical for the enhance­ment of glutathione and glutathione-related enzyme activity and the protection of rice from pretilachlor injury.

Effects of the Deer Antler Extract on Scopolamine-induced Memory Impairment and Its Related Enzyme Activities

2009 ◽  
Vol 38 (4) ◽  
pp. 409-414 ◽  
Author(s):  
Mi-Ra Lee ◽  
Bai-Shen Sun ◽  
Li-Juan Gu ◽  
Chun-Yan Wang ◽  
Zhe-Ming Fang ◽  
...  
Keyword(s):  
Enzyme Activities ◽  
Memory Impairment ◽  
Deer Antler ◽  
Related Enzyme

CHANGES IN SUGAR LEVEL AND RELATED ENZYME ACTIVITY OF ARBUSCULAR MYCORRHIZAL ASPARAGUS

2002 ◽  
pp. 315-321
Author(s):  
M. Akiyama ◽  
T. Suzuki ◽  
K. Oosawa ◽  
I. Maezaki ◽  
N. Shiomi
Keyword(s):  
Enzyme Activity ◽  
Arbuscular Mycorrhizal ◽  
Related Enzyme

Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana

2001 ◽  
Vol 29 (2) ◽  
pp. 283-286 ◽  
Author(s):  
E. L. Rylott ◽  
M. A. Hooks ◽  
I. A. Graham
Keyword(s):  
Arabidopsis Thaliana ◽  
Enzyme Activities ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Molecular Genetic ◽  
Regulation Of Gene Expression ◽  
Growth Period ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

Molecular genetic approaches in the model plant Arabidopsis thaliana (ColO) are shedding new light on the role and control of the pathways associated with the mobilization of lipid reserves during oilseed germination and post-germinative growth. Numerous independent studies have reported on the expression of individual genes encoding enzymes from the three major pathways: β-oxidation, the glyoxylate cycle and gluconeogenesis. However, a single comprehensive study of representative genes and enzymes from the different pathways in a single plant species has not been done. Here we present results from Arabidopsis that demonstrate the co-ordinate regulation of gene expression and enzyme activities for the acyl-CoA oxidase- and 3-ketoacyl-CoA thiolasemediated steps of β-oxidation, the isocitrate lyase and malate synthase steps of the glyoxylate cycle and the phosphoenolpyruvate carboxykinase step of gluconeogenesis. The mRNA abundance and enzyme activities increase to a peak at stage 2, 48 h after the onset of seed germination, and decline thereafter either to undetectable levels (for malate synthase and isocitrate lyase) or low basal levels (for the genes of β-oxidation and gluconeogenesis). The co-ordinate induction of all these genes at the onset of germination raises the possibility that a global regulatory mechanism operates to induce the expression of genes associated with the mobilization of storage reserves during the heterotrophic growth period.

Avenanthramide content and related enzyme activities in oats as affected by steeping and germination

2008 ◽  
Vol 48 (2) ◽  
pp. 294-303 ◽  
Author(s):  
Maria Skoglund ◽  
David M. Peterson ◽  
Roger Andersson ◽  
Janicka Nilsson ◽  
Lena H. Dimberg
Keyword(s):  
Enzyme Activities ◽  
Related Enzyme
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