Molecular and whole-plant responses to selection for enzyme activity in alfalfa root nodules: evidence for molecular compensation of aspartate aminotransferase expression

1992 ◽  
Vol 84-84 (3-4) ◽  
pp. 355-361 ◽  
Author(s):  
M. W. Farnham ◽  
N. R. Degenhart ◽  
C. P. Vance ◽  
D. K. Barnes
Keyword(s):  
Enzyme Activity ◽  
Aspartate Aminotransferase ◽  
Root Nodules ◽  
Plant Responses ◽  
Whole Plant ◽  
Selection For ◽  
Alfalfa Root

scholarly journals Aspartate Aminotransferase in Alfalfa Root Nodules

1990 ◽  
Vol 94 (4) ◽  
pp. 1634-1640 ◽  
Author(s):  
Mark W. Farnham ◽  
Stephen M. Griffith ◽  
Susan S. Miller ◽  
Carroll P. Vance
Keyword(s):  
Aspartate Aminotransferase ◽  
Root Nodules ◽  
Alfalfa Root

scholarly journals Aspartate Aminotransferase in Alfalfa Root Nodules

1989 ◽  
Vol 90 (4) ◽  
pp. 1622-1629 ◽  
Author(s):  
Stephen M. Griffith ◽  
Carroll P. Vance
Keyword(s):  
Aspartate Aminotransferase ◽  
Root Nodules ◽  
Alfalfa Root

Target-Site Resistance to Nicosulfuron in Johnsongrass (Sorghum halepense) from Chilean Corn Fields

Weed Science ◽  
2015 ◽  
Vol 63 (3) ◽  
pp. 631-640 ◽  
Author(s):  
María J. Hernández ◽  
Rocío León ◽  
Albert J. Fischer ◽  
Marlene Gebauer ◽  
Rafael Galdames ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Consensus Sequence ◽  
Target Site ◽  
Sorghum Halepense ◽  
Acetohydroxyacid Synthase ◽  
Sequencing Analysis ◽  
Whole Plant ◽  
Target Site Resistance ◽  
Selection For

Johnsongrass is a common weed of corn in Chile, which is most often controlled by nicosulfuron, an acetohydroxyacid synthase (AHAS)-inhibiting herbicide. Recurrent nicosulfuron use has resulted in selection for resistant johnsongrass biotypes. We conducted studies to determine nicosulfuron resistance levels in two johnsongrass biotypes from Chile and to investigate if this resistance was target-site mediated. Whole-plant resistance to nicosulfuron was 33 and 46 times higher in resistant (R) than in susceptible (S) plants grown from seed and rhizomes, respectively. The nicosulfuron concentrations for 50% inhibition of AHAS enzyme activity in vitro were more than 11 times higher in R than in S plants. Sequencing analysis of theAHAScoding sequence revealed a Trp-574-Leu substitution in both R biotypes. This study shows that resistance to nicosulfuron in the two R biotypes is conferred by an altered target site. We also report the first consensus sequence of the johnsongrassAHASgene corresponding to the known mutation sites conferring resistance to AHAS-inhibiting herbicides.

scholarly journals Aspartate Aminotransferase in Alfalfa Root Nodules

1990 ◽  
Vol 93 (2) ◽  
pp. 603-610 ◽  
Author(s):  
Mark W. Farnham ◽  
Susan S. Miller ◽  
Stephen M. Griffith ◽  
Carroll P. Vance
Keyword(s):  
Aspartate Aminotransferase ◽  
Root Nodules ◽  
Alfalfa Root

scholarly journals Analysis of enzyme activity and the level of malondialdehyde in the saliva of children with gingivitis

2009 ◽  
Vol 66 (11) ◽  
pp. 892-896
Author(s):  
Olivera Trickovic-Janjic ◽  
Tatjana Cvetkovic ◽  
Mirjana Apostolovic ◽  
Draginja Kojovic ◽  
Ljiljana Kostadinovic ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Study Groups ◽  
Functional Condition ◽  
Gamma Glutamyl Transferase ◽  
Gamma Glutamyl ◽  
Severe Inflammation ◽  
Glutamyl Transferase

Introduction/Aim. By analyzing activity of some of the enzymes normally present in the saliva and the level of malondialdehyde in gingivitis, it is possible to estimate the functional condition of parodontium, and the examined parameters can be considered as biochemical markers of its functional condition. The aim of this paper was to examine activity of alanine aminotransferase, aspartate aminotransferase, gamma glutamyl transferase, lactate dehydrogenase and the level of malondialdehyde in the saliva of children affected with gingivitis, as well as the values of the mentioned parameters in relation to the level of the inflammation of gingiva. Methods. The research included 120 children at the age of 12.2 with permanent dentition. L?e and Silness gingival index was used to estimate the condition of gingiva, based on which the children were classified into four groups: the children with healthy gingiva (the control groups), the children with mild, moderate and severe inflammation of gingiva (the study group). Enzymes of the saliva were determined by the use of original tests and measured by the autoanalyser (Bio Systems A25, Spain). A modified method with tiobarbituric acid was used to determine malondialdehyde in nonstimulated mixed saliva. Results. The results of the examined enzyme activity and the level of malondialdehyde in the saliva of the study groups showed statistically considerably higher values for the level of malondialdehyde (p < 0.001), for the activity of aspartate aminotransferase and gamma glutamyl transferase (p < 0.01), as well as for alanine aminotransferase (p < 0.05) in comparison with the control group, whereas the activity of lactate dehydrogenase did not show a statistically significant increase. In relation to the level of the inflammation of gingiva, the results of the examination of the enzyme activity in the study groups showed statistically significantly higher values in the group with severe inflammation in comparison with those with mild, as well as the moderate inflammatory, except for the gamma glutamyl transferase, and in the group with moderate inflammation compared to that with the mild one, except for alanine aminotransferase. The results of the examination of the level of malondialdehyde in the saliva of the study groups did not show a statistically significantly increase in relation to the level of the inflammation of gingiva. Conclusion. There is a higher level of alanine aminotransferase, aspartate aminotransferase, gamma glutamyl transferase and lactate dehydrogenase enzyme activity together with the higher level of malondialdehyde in the saliva of children with gingivitis in comparison with the activity of the same enzymes and the level of malondialdehyde in the saliva of children without gingivitis. The activity of the examined enzymes in the saliva of children with gingivitis increases in relation to the intensity of the pathological process, whereas the level of malondialdehyde shows no significant difference in relation to the level of the inflammation of gingiva.

Resistance in Smallflower Umbrella Sedge (Cyperus difformis L.) to Acetolactate Synthase-Inhibiting Herbicides in Rice - First Case in India

2021 ◽  
pp. 1-22
Author(s):  
Vijay K. Choudhary ◽  
Seshadri S. Reddy ◽  
Subhash K. Mishra ◽  
Bhumesh Kumar ◽  
Yogita Gharde ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Acetolactate Synthase ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Synthetic Auxin ◽  
Cyperus Difformis ◽  
First Case ◽  
Whole Plant ◽  
Plant Bioassay ◽  
Direct Seeded

Abstract Smallflower umbrella sedge is one of the problematic weeds in direct-seeded rice in India. Bispyribac-sodium (acetolactate synthase-inhibiting herbicide) is a commonly used in rice, but recently growers have reported lack of smallflower umbrella sedge control with this herbicide. An extensive survey was carried out in two rice growing states, Chhattisgarh and Kerala, where 53 putative bispyribac-sodium resistant (BR) biotypes were collected. Studies were conducted to confirm resistance to bispyribac-sodium and to test the efficacy of newly developed synthetic auxin herbicide florpyrauxifen-benzyl on putative BR biotypes. Whole-plant bioassay revealed that bispyribac-sodium is no longer effective. Of 53 putative BR biotypes, 17 biotypes survived recommended label rate of 25 g ai ha−1. Effective bispyribac-sodium rate required to control 50% of the plants in most of the BR biotypes (ED50) ranged from 19 to 96 g ha−1 whereas it was 10 g ha−1 in susceptible biotype. In two highly resistant biotypes, ED50 was beyond the maximum tested rate, 200 g ha−1. This suggests 2 to >20-fold resistance in BR biotypes. Acetolactate synthase (ALS) enzyme activity assay suggests altered target site as mechanism of resistance to bispyribac-sodium. This study confirms the first case of evolved resistance in smallflower umbrella sedge for bispyribac-sodium in India. However, the newly developed synthetic auxin, florpyrauxifen-benzyl effectively controlled all BR biotypes at the field use rate 31.25 g ae ha−1.

The effects of ethanol (0.75 g/kg body weight) on the activities of selected enzymes in sera of healthy young adults: 1. Intermediate-term effects.

1977 ◽  
Vol 23 (5) ◽  
pp. 830-834 ◽  
Author(s):  
D E Freer ◽  
B E Statland
Keyword(s):  
Young Adults ◽  
Body Weight ◽  
Enzyme Activity ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Ethanol Ingestion ◽  
Similar Time ◽  
Gamma Glutamyltransferase ◽  
Time Courses ◽  
Apparently Healthy

Abstract We report the intermediate-term effects of three consecutive evenings of moderate ethanol ingestion (0.75 g/kg body weight each evening) on activity values for alkaline phosphatase, gamma-glutamyltransferase, creatine kinase, aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase in sera of nine apparently healthy young adults. We define "intermediate-term" effects as those occurring between 10 h and 100 h after completion of the ethanol consumption schedule. The most pronounced changes in enzyme activity for the group of volunteers were: gamma-glutamyltransferase, +25% at 60 h after ethanol ingestion; alanine aminotransferase, +12% at 60 h after ethanol; and aspartate aminotransferase,--12% at 60 h after ethanol. All three enzymes exhibited similar time courses, i.e., mean peak activity changes were observed at 60 h, and all three mean enzyme activity values returned to near baseline by 100 h. The possible explanations for the observed changes and the clinical significance are discussed.

scholarly journals Effect of Various Diluents on the Activity of Several Enzymes Present in Serum

1973 ◽  
Vol 19 (9) ◽  
pp. 1079-1080
Author(s):  
Ted W Fendley ◽  
Jane M Hochholzer ◽  
Christopher S Frings
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Confidence Level ◽  
Aspartate Aminotransferase ◽  
Nacl Solution ◽  
Manual Method ◽  
Accuracy And Precision ◽  
Significant Difference

Abstract We have evaluated the effect of diluting serum with water or NaCl solution (8.5 or 9.0 g/liter) before assaying by a manual method for creatine kinase (EC 2.7.3.2), alkaline phosphatase (EC 3.1.3.1), lactate dehydrogenase (EC 1.1.1.27), and aspartate aminotransferase (EC 2.6.1.1) activity. The t test and the F test show no significant difference in the accuracy and precision of the assays at the 95% confidence level when 100 different samples were compared for each enzyme activity after use of the three diluents.

Column-chromatographic separation of isoenzymes of aspartate aminotransferase.

1978 ◽  
Vol 24 (10) ◽  
pp. 1805-1812 ◽  
Author(s):  
E J Sampson ◽  
S A Miller ◽  
S S McKneally ◽  
V S Whitner ◽  
W H Hannon ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Human Serum ◽  
Aspartate Aminotransferase ◽  
Chromatographic Method ◽  
Human Origin ◽  
Additional Information ◽  
Bed Height ◽  
Optimized Conditions ◽  
Column Chromatographic

Abstract We describe a column-chromatographic method for separating the mitochondrial and cytoplasmic isoenzymes of aspartate aminotransferase in human serum. Bed height of the ion exchanger, pH, and salt concentrations in the eluting buffers are shown to be variables affecting the separation of the isoenzymes. Under the optimized conditions selected for this study, a 30% increase in volume was observed in one fraction, associated with changing the salt concentration of the eluting buffer and attributed to a contraction of the DEAE-Sephadex A-50. Elution profiles (enzyme activity vs. fraction number) were examined with highly purified mitochondrial and cytoplasmic isoenzymes of human origin in bovine serum albumin and human serum. Recovery of the enzyme in the eluted fractions averaged 102% (SD, 2.0%) for specimens prepared from the purified isoenzymes and 104% (SD, 10.7%) for 38 human serum specimens. The separation technique showed linearity to catalytic concentrations in excess of 200 U/liter (reaction temperature 30 degrees C) for each isoenzyme. Additional information is presented regarding among-day precision and the effect of specimen dilution.

Sign in / Sign up

Export Citation Format

Share Document