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H H H C O H C OH ATP ADP H C OH H CH O HO C H H C OH H C H C OH HO C C OH H C OHO H OH H C H – O –O OP H C C HO C H C C C H H O H C OPO C O O H O OH HO C H H C OPO O H C O O H HO C H OH H C OH H OH – O H C OH H OPO H H C OPO H H C O H C OH H C OPO H OPO O O ATP ADP C O OPO H C OH OPO H C OPO H – O C H C OH H C H – O C C C O C H C H C OH H – O ATP ADP O H H H – Dihydroxyacetone phosphate Glyceraldehyde Glucose Glucose 6-phosphate Fructose 6-phosphate Fructose 1, 6-phosphate 3-phosphate 2× NAD O C H C O H C H H OPO H2O Pyruvate Phosphoenolpyruvate (PEP) 2-phosphoglycerate 3-phosphoglycerate 1,3-bisphosphoglycerate + NADH + H + ATP ADP Fructose Triose bisphosphate phosphate Hexokinase Phosphoglucose Phosphofructo aldose isomerase isomerase kinase O Glycolysis Glyceraldehyde 3-phosphate dehydrogenase + Pi Pyruvate kinase Enolase Phosphoglycerate Phosphoglycerate mutase kinase – O – O – O – O – O – O – O – O – O – O – O – O – O – O – Fig. 1.1. Glycolysis pathway (it consists of 10 steps, each catalyzed by an enzyme). This is a universal pathway (Fig. 1.1) for the breakdown of glucose (a hexose, 6C) to two molecules of triose (3C) that occurs in all types of biological cells. Glycolysis has a 10-step biochemical pathway: Step 1: Glucose is converted to glucose-6-phosphate catalyzed by a hexokinase with energy provided by an ATP. Step 2: Glucose-6-phosphate is isomerized to fructose-6-phosphate in the presence of phosphoglucose isomerase. Step 3: Fructose-6-phosphate is converted to fructose 1, 6-bisphosphate catalyzed by phosphofructokinase with energy provided by a second molecule of ATP. Step 4: Fructose 1, 6-bisphosphate is then split into two triose molecules—dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, catalyzed by a fructose bisphosphate aldolase. Step 5: Dihydroxyacetone phosphate is isomerized to glyceraldehyde 3-phosphate in a reversible reaction catalyzed by triose phosphate isomerase—in theory, a glucose molecule can yield two 3-glyceraldehyde molecules via steps 4 and 5. Step 6: Glyceraldehyde 3-phosphate is converted to 1,3-bisphosphoglycerate with the addition of a molecule of inorganic phosphate (P i ) catalyzed by glyceraldehyde phosphate dehydrogenase in the presence of a cofactor NAD + , which is reduced to NADH + H + + 2é. Step 7: 1,3-bisphosphoglycerate is transformed to 3-phosphoglycerate catalyzed by phosphoglycerate kinase with the production of a molecule of ATP from ADP. 6 K.L. Heong, K.H. Tan, C.P.F. Garcia, L.T. Fabellar, and Z. Lu
Step 8: 3-phosphoglycerate is isomerized to 2-phosphoglycerate catalyzed by phosphoglycerate mutase. Step 9: 2-phosphoglycerate is changed to phosphoenolpyruvate catalyzed by enolase with a release of a molecule of water. Step 10: Phosphoenolpyruvate is fi nally converted to pyruvate in the presence of pyruvate kinase with the synthesis of a high-energy molecule (ATP) from ADP. A molecule of glucose after undergoing glycolysis has a net yield of two molecules each of pyruvate, water, NADH + H + + 2é (this cofactor carrying two electrons can be used to produce three molecules of ATP—to be discussed later), and ATP. Therefore, in terms of the number of high-energy molecules produced through glycolysis, a molecule of glucose produces eight molecules of ATP. Pyruvate, the end product of glycolysis, is used (Fig. 1.2) in (1) the process of fermentation catalyzed by pyruvate dehydrogenase in yeast and plants to produce ethanol; or (2) processes that demand quick and immediate energy in the absence of oxygen (during anaerobic activity such as vigorous exercise) in the presence of lactate dehydrogenase to form lactate—which accumulates, leading to muscular fatigue during “oxygen debt”; or (3) in most cells it enters the mitochondrion during cellular respiration, in the presence of Coenzyme A (CoA) catalyzed by pyruvate dehydrogenase complex (Mg ++ , thiamine pyrophosphate, lipoic acid, and transacetylase) to form acetyl-CoA. Then, the acetyl-CoA enters the Kreb’s cycle, in which the acetate portion of the molecule is completely metabolized to be released as water and carbon dioxide. Kreb’s cycle [citric acid/tricarboxylic acid (TCA) cycle] This is a continuous metabolic cycle that occurs in the matrix of a mitochondrion as long as there is a constant supply of acetyl-CoA from either glucose through glycolysis or fatty acids through ß-oxidation (to be discussed later). This metabolic cycle also consists of 10 enzymic steps (Fig. 1.2): Step 1: Acetyl-CoA fi rst enters the cycle by combining with oxaloacetic acid in the presence of citrate synthetase and a molecule of water to form citric acid. Step 2: Citric acid is transformed into cis-aconitic acid by the removal of a molecule of water catalyzed by aconitase. Step 3: cis-aconitic acid is quickly changed to isocitric acid through the addition of a water molecule still in the presence of the enzyme aconitase. Step 4: Isocitric acid in the presence of NAD + cofactor and isocitric acid dehydrogenase is converted to oxalosuccinic acid and yields a reduced cofactor (NADH + + H + + 2é). Step 5: Oxalosuccinic acid is transformed to α-ketoglutaric acid catalyzed by oxaloacetic acid decarboxylase with the removal and release of a molecule of carbon dioxide. Step 6: α-ketoglutaric acid with a removal and release of a carbon dioxide molecule catalyzed by α-ketoglutarate dehydrogenase combines with a CoA to form succinyl-CoA. Research methods in toxicology and insecticide resistance monitoring of rice planthoppers 7
Page 2 and 3: Research Methods in Toxicology and
Page 4 and 5: Contents Foreword v Preface vii Ack
Page 6: Foreword By 2020, the world will re
Page 9 and 10: synergistic, antagonistic, or no ad
Page 11 and 12: CHAPTER 1: Introduction to insect t
Page 13 and 14: Toxicology (derived from two Greek
Page 15: ogy can be subdivided into many sub
Page 19 and 20: Each pyruvate molecule when complet
Page 21 and 22: H + H + H + H + NADH Cytochrome c d
Page 23 and 24: Insect physiology Mitochondria A mi
Page 25 and 26: of sodium channels allowing sodium
Page 27 and 28: ) Cytosol Pretranslation Masking, d
Page 29 and 30: CHAPTER 2: Insecticide toxicology R
Page 31 and 32: An insecticide is a pesticide used
Page 33 and 34: 2. Application technique, for examp
Page 35 and 36: nant in insects. In the neurons, th
Page 37 and 38: 30 g/kg, and fenoxycarb, LD 50 16.8
Page 39 and 40: tive feedback of acetylcholine rele
Page 41 and 42: Metabolic resistance via detoxifica
Page 43 and 44: 5. pen—a recessive gene that decr
Page 45 and 46: 1. Use of an appropriate synergist,
Page 47 and 48: CHAPTER 3: Quantal response data an
Page 49 and 50: Insecticide research generally invo
Page 51 and 52: esponse to probits is available in
Page 53 and 54: CHAPTER 4: Rearing and preparation
Page 55 and 56: As discussed in Chapter 3, for expe
Page 57 and 58: 4.3 4.4 Fig. 4.3. Aluminum rearing/
Page 59 and 60: Preparation of standardized test in
Page 61 and 62: CHAPTER 5: Preparation of test solu
Page 63 and 64: The median lethal dose (LD 50 ) of
Page 65 and 66: Fig. 5.3. Recovery cage preparation
Page 67 and 68:
Fig. 5.6. Treated planthoppers are
Page 69 and 70:
CHAPTER 6: Analyz ing quantal respo
Page 71 and 72:
In Chapter 3, we discussed probit a
Page 73 and 74:
3. There is a need to further forma
Page 75 and 76:
Using PoloPlus© The quantal respon
Page 77 and 78:
Fig. 6.1. Output results. Research
Page 79 and 80:
The values of the variance-covarian
Page 81 and 82:
The lethal dose ratio on lines 95-9
Page 83 and 84:
8. Then, Paste the Excel data sets
Page 85 and 86:
3. For the fi rst population, open
Page 87 and 88:
5. Highlight and Copy the Probit va
Page 89 and 90:
9. Right-click the y-axis, and clic
Page 91 and 92:
CHAPTER 7: Analyzing joint action o
Page 93 and 94:
PoloMix© is another software devel
Page 95 and 96:
c. Lastly, on the File menu, the Sa
Page 97 and 98:
Fig. 7.2. PoloMix© output. Researc
Page 99 and 100:
CHAPTER 8: Presenting results Resea
Page 101 and 102:
The previous chapters provide the m
Page 103 and 104:
References Abbott WS. 1925. A metho
Page 105 and 106:
Sudderudin KI, Tan KH. 1973. Some h
Page 107 and 108:
Appendix A Table 1. Transformation
Page 109 and 110:
Appendix Table B1. Raw data recordi
Page 111:
Appendix C Table 1. The distributio
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