Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90192-N
Divina E. Santos, Hiroshi Takeuchi
1. The pneumatic pressure ejection of achatin-I (Gly-d-Phe-l-Ala-l-Asp), an endogenous tetrapeptide having a d-phenylalanine residue, produced an inward current (Iin) in an identifiable giant neuron, PON (periodically oscillating neuron), of an African giant snail, Achatina fulica Férussac. The influence of the drugs for membrane excitability modification, applied by perfusion, on the PON excitation caused by achatin-I was examined under voltage clamp.
2. The four channel blocking drugs, tetrodotoxin (TTX), tetraethylammonium chloride (TEA), verapamil and picrotoxin, at 10,−4 M did not affect significantly the PON excitation caused by the peptide.
3. (BPLT), a membrane hyperpolarizant, at 10−6 M and concanavalin A (Con A), which altered the response to l-glutamate, at 100 were considered to hardly influence the PON excitation caused by achatin-I.
1. 气压喷射一种内源性四肽,含有d-苯基丙氨酸残基的Achatina - i (gly -d- phel - ala -l- asp),在非洲大蜗牛Achatina fulica f russac的可识别的巨大神经元PON(周期性振荡神经元)中产生向内电流(Iin)。在电压箝位下,观察灌注膜兴奋性修饰药物对achatin-I引起的PON兴奋的影响。4种通道阻断药物河豚毒素(TTX)、四乙基氯化铵(TEA)、异拉帕米和微毒素在10、−4 M时对肽引起的PON兴奋无显著影响。膜超极化剂N-β-苯基丙炔- l-酪氨酸(BPLT)在10−6 M和改变l-谷氨酸反应的豆豆蛋白a (Con a)在100 μgml−1时被认为几乎不影响紫菜素- 1引起的PON兴奋。
{"title":"Influence of the drugs for membrane excitability modification on the excitation caused by achatin-I","authors":"Divina E. Santos, Hiroshi Takeuchi","doi":"10.1016/0742-8413(93)90192-N","DOIUrl":"10.1016/0742-8413(93)90192-N","url":null,"abstract":"<div><p>1. The pneumatic pressure ejection of achatin-I (Gly-<span>d</span>-Phe-<span>l</span>-Ala-<span>l</span>-Asp), an endogenous tetrapeptide having a <span>d</span>-phenylalanine residue, produced an inward current (<em>I</em><sub>in</sub>) in an identifiable giant neuron, PON (periodically oscillating neuron), of an African giant snail, <em>Achatina fulica</em> Férussac. The influence of the drugs for membrane excitability modification, applied by perfusion, on the PON excitation caused by achatin-I was examined under voltage clamp.</p><p>2. The four channel blocking drugs, tetrodotoxin (TTX), tetraethylammonium chloride (TEA), verapamil and picrotoxin, at 10,<sup>−4</sup> M did not affect significantly the PON excitation caused by the peptide.</p><p>3. <span><math><mtext>N-β-</mtext><mtext>phenylpropionyl-</mtext><mtext>L</mtext><mtext>-tyrosine</mtext></math></span> (BPLT), a membrane hyperpolarizant, at 10<sup>−6</sup> M and concanavalin A (Con A), which altered the response to <span>l</span>-glutamate, at 100 <span><math><mtext>μg</mtext><mtext>ml</mtext><msup><mi></mi><mn>−1</mn></msup></math></span> were considered to hardly influence the PON excitation caused by achatin-I.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 185-188"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90192-N","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18693446","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90208-3
Akinori Hirashima , Morifusa Eto
1. Various biogenic amines including octopamine, dopamine and serotonin, and their precursors and metabolites in haemolymph and the central nervous system from American cockroaches (Periplaneta americana L.) were measured using electrochemical detection.
2. Octopamine was found in similar high relative abundances in haemolymph and the central nervous system.
3. The amount of octopamine was much higher than that of tyramine and synephrine in haemolymph and thoracic nerve cord, whereas tyramine was at the highest level followed by octopamine and synephrine in the brain.
4. Insects were stressed by vibrating at 100 or 1000 Hz, visually by flashing light at 4 Hz for 15 min or by immersing the insect in water at 60°C for 30 sec, which resulted in the elevation of octopamine, tyramine, synephrine and tyrosine levels in thoracic nerve cord.
{"title":"effect of stress on levels of octopamine, dopamine and serotonin in the American cockroach (Periplaneta americana L.)","authors":"Akinori Hirashima , Morifusa Eto","doi":"10.1016/0742-8413(93)90208-3","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90208-3","url":null,"abstract":"<div><p>1. Various biogenic amines including octopamine, dopamine and serotonin, and their precursors and metabolites in haemolymph and the central nervous system from American cockroaches (<em>Periplaneta americana</em> L.) were measured using electrochemical detection.</p><p>2. Octopamine was found in similar high relative abundances in haemolymph and the central nervous system.</p><p>3. The amount of octopamine was much higher than that of tyramine and synephrine in haemolymph and thoracic nerve cord, whereas tyramine was at the highest level followed by octopamine and synephrine in the brain.</p><p>4. Insects were stressed by vibrating at 100 or 1000 Hz, visually by flashing light at 4 Hz for 15 min or by immersing the insect in water at 60°C for 30 sec, which resulted in the elevation of octopamine, tyramine, synephrine and tyrosine levels in thoracic nerve cord.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 279-284"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90208-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90191-M
Shiko Chichibu, Atsushi Chiba
1. Changes in the amounts of mucus secreted by the epidermis of the slug in response to an irritant chemical substance (NaCl) and the effect of mechanical stimulation on high-energy phosphorylation metabolism were studied.
2. 31P signals obtained from the slug with in vivo31P nuclear magnetic resonance (NMR) spectroscopy included phosphonate, sugar phosphate (SP), inorganic phosphate (Pi), arginine phosphate (Arg-P), and ATP (γ, α and β).
3. When the slug epidermis came into contact with NaCl or was exposed to mechanical stimulation, the concentration of Arg-P decreased and that of Pi increased along with mucus secretion.
4. The change of 31P signals in response to chemical stimulation was much more variable than that in response to mechanical stimulation.
5. The β-ATP concentration was dependent on the amount of mucus secreted.
{"title":"Changes of 31P metabolism during mucus secretion in the slug (Incilaria bilineata)","authors":"Shiko Chichibu, Atsushi Chiba","doi":"10.1016/0742-8413(93)90191-M","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90191-M","url":null,"abstract":"<div><p>1. Changes in the amounts of mucus secreted by the epidermis of the slug in response to an irritant chemical substance (NaCl) and the effect of mechanical stimulation on high-energy phosphorylation metabolism were studied.</p><p>2. <sup>31</sup>P signals obtained from the slug with <em>in vivo</em><sup>31</sup>P nuclear magnetic resonance (NMR) spectroscopy included phosphonate, sugar phosphate (SP), inorganic phosphate (Pi), arginine phosphate (Arg-P), and ATP (γ, α and β).</p><p>3. When the slug epidermis came into contact with NaCl or was exposed to mechanical stimulation, the concentration of Arg-P decreased and that of Pi increased along with mucus secretion.</p><p>4. The change of <sup>31</sup>P signals in response to chemical stimulation was much more variable than that in response to mechanical stimulation.</p><p>5. The β-ATP concentration was dependent on the amount of mucus secreted.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 179-183"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90191-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136598185","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90214-6
Abdulaziz A. Al-Jafari
1. The camel erythrocyte membrane bound acetylcholinesterase (AChE) was extracted with the non-ionic detergent Triton X-100 and some of its kinetics parameters were studied. In addition the effect of tetracaine hydrochloride on AChE was also investigated.
2. The Michaelis-Menten constant (Km) for the hydrolysis of acetylthiocholine iodide was found to be 7 × 10−5M and the Vmax was 21.2 μmol/hr/mg protein.
3. Tetracaine (0.025–0.80 mM) reversibly inhibited the AChE activity (25–82%) in a concentration-dependent manner, the ic50 being about 0.12 mM.
4. The Lineweaver-Burk plot and its secondary plots indicated that the nature of this inhibition is of the linear mixed type. This mixed type inhibition system is considered to be composed of partial competitive and pure non-competitive in nature.
5. The values of Ki(slope) and Kii(intercept) were estimated as 0.127 mM and 0.263 mM, respectively, by a secondary replot of primary double reciprocal plot of Lineweaver-Burk plot and Dixon plot.
6. ratio shows that tetracaine has a greater affinity of binding to the active site than to a peripheral site.
{"title":"Investigation of the reversible inhibition of camel (Camelus dromedarius) acetylcholinesterase by tetracaine","authors":"Abdulaziz A. Al-Jafari","doi":"10.1016/0742-8413(93)90214-6","DOIUrl":"10.1016/0742-8413(93)90214-6","url":null,"abstract":"<div><p>1. The camel erythrocyte membrane bound acetylcholinesterase (AChE) was extracted with the non-ionic detergent Triton X-100 and some of its kinetics parameters were studied. In addition the effect of tetracaine hydrochloride on AChE was also investigated.</p><p>2. The Michaelis-Menten constant (<em>K</em><sub><span>m</span></sub>) for the hydrolysis of acetylthiocholine iodide was found to be 7 × 10<sup>−5</sup>M and the <em>V</em><sub>max</sub> was 21.2 μmol/hr/mg protein.</p><p>3. Tetracaine (0.025–0.80 mM) reversibly inhibited the AChE activity (25–82%) in a concentration-dependent manner, the <span>ic</span><sub>50</sub> being about 0.12 mM.</p><p>4. The Lineweaver-Burk plot and its secondary plots indicated that the nature of this inhibition is of the linear mixed type. This mixed type inhibition system is considered to be composed of partial competitive and pure non-competitive in nature.</p><p>5. The values of <em>K</em><sub>i(slope)</sub> and <em>K</em><sub>ii(intercept)</sub> were estimated as 0.127 mM and 0.263 mM, respectively, by a secondary replot of primary double reciprocal plot of Lineweaver-Burk plot and Dixon plot.</p><p>6. <span><math><mtext>K</mtext><msub><mi></mi><mn><mtext>ii</mtext></mn></msub><mtext>K</mtext><msub><mi></mi><mn><mtext>i</mtext></mn></msub></math></span> ratio shows that tetracaine has a greater affinity of binding to the active site than to a peripheral site.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 323-327"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90214-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90188-Q
Kazuaki Takahashi, Yukio Akiba, Masaaki Horiguchi
1. Most of the components of the mixed function oxidase (MFO) in hepatic microsomes were reduced by corticosterone implants, and the degree of the reduction in females and at an older age was greater than those in males and at a younger age.
2. Ascorbic acid (AA) prevented the reduction in the MFO caused by corticosterone implants.
3. The activities of aniline hydroxylase and aminopyrine N-demethylase were enhanced by corticosterone implants regardless of AA supplementation.
4. The activity of NADPH-cytochrome c reductase in male broiler was greater than that in females under normal conditions.
5. Corticosterone implants and dietary AA had less influence on the antibody production, especially to T-cell dependent antigen.
{"title":"Sex-related differences of hepatic microsomal mixed function oxidase system and antibody production in broilers implanted with corticosterone and/or fed ascorbic acid","authors":"Kazuaki Takahashi, Yukio Akiba, Masaaki Horiguchi","doi":"10.1016/0742-8413(93)90188-Q","DOIUrl":"10.1016/0742-8413(93)90188-Q","url":null,"abstract":"<div><p>1. Most of the components of the mixed function oxidase (MFO) in hepatic microsomes were reduced by corticosterone implants, and the degree of the reduction in females and at an older age was greater than those in males and at a younger age.</p><p>2. Ascorbic acid (AA) prevented the reduction in the MFO caused by corticosterone implants.</p><p>3. The activities of aniline hydroxylase and aminopyrine <em>N</em>-demethylase were enhanced by corticosterone implants regardless of AA supplementation.</p><p>4. The activity of NADPH-cytochrome <em>c</em> reductase in male broiler was greater than that in females under normal conditions.</p><p>5. Corticosterone implants and dietary AA had less influence on the antibody production, especially to T-cell dependent antigen.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 159-164"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90188-Q","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90190-V
Marisa Manzano , Paolo Romandini , Marco De Bertoldi , Mariano Beltramini , Benedetto Salvato , Ivo Cozzani
1. Three strains of Saccharomyces cerevisiae have been exposed to methanol both in the presence and absence of heavy metal ions. The growth curves and the Superoxide dismutase activity were determined.
2. The presence of alcohol, copper or cadmium alone did not give strong cytotoxic effects, while methanol plus cadmium yielded a growth inhibition in two strains.
3. SOD levels were stimulated by copper, while methanol did not affect SOD in this non-methylotrophic yeast, indicating the need of alcohol assimilation to stimulate SOD. Cadmium had no inducing effects on SOD levels.
{"title":"Interaction among heavy metals and methanol affecting superoxide dismutase activity in Saccharomyces cerevisiae","authors":"Marisa Manzano , Paolo Romandini , Marco De Bertoldi , Mariano Beltramini , Benedetto Salvato , Ivo Cozzani","doi":"10.1016/0742-8413(93)90190-V","DOIUrl":"10.1016/0742-8413(93)90190-V","url":null,"abstract":"<div><p>1. Three strains of <em>Saccharomyces cerevisiae</em> have been exposed to methanol both in the presence and absence of heavy metal ions. The growth curves and the Superoxide dismutase activity were determined.</p><p>2. The presence of alcohol, copper or cadmium alone did not give strong cytotoxic effects, while methanol plus cadmium yielded a growth inhibition in two strains.</p><p>3. SOD levels were stimulated by copper, while methanol did not affect SOD in this non-methylotrophic yeast, indicating the need of alcohol assimilation to stimulate SOD. Cadmium had no inducing effects on SOD levels.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 175-178"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90190-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19096862","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90211-3
Giorgio Venturini
1. The adenylate cyclase activity present in the particulate fraction of planaria homogenates has been characterized.
2. The enzyme requires divalent cations (Mg2+), and a Km for ATP of 0.58 at 30°C was measured.
3. GTP and Gpp(NH)p, in an optimal range of 10−4–10−5M, increase the enzymatic activity.
4. In the presence of GTP, dopamine stimulates the adenylate cyclase and its action is inhibited by dopaminergic antagonist.
5. Both D-1 and D-2 selective dopaminergic agonists stimulate the enzymatic activity and their action is selectively antagonized by D-1 and D-2 antagonists.
6. The high concentrations required for some D-1 and D-2 agents to be effective, suggest an only partial consistency with mammalian dopaminergic receptors.
{"title":"Dopamine sensitive adenylate cyclase in planaria Dugesia gonocephala","authors":"Giorgio Venturini","doi":"10.1016/0742-8413(93)90211-3","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90211-3","url":null,"abstract":"<div><p>1. The adenylate cyclase activity present in the particulate fraction of planaria homogenates has been characterized.</p><p>2. The enzyme requires divalent cations (Mg<sup>2+</sup>), and a <em>K</em><sub>m</sub> for ATP of 0.58 at 30°C was measured.</p><p>3. GTP and Gpp(NH)p, in an optimal range of 10<sup>−4</sup>–10<sup>−5</sup>M, increase the enzymatic activity.</p><p>4. In the presence of GTP, dopamine stimulates the adenylate cyclase and its action is inhibited by dopaminergic antagonist.</p><p>5. Both D-1 and D-2 selective dopaminergic agonists stimulate the enzymatic activity and their action is selectively antagonized by D-1 and D-2 antagonists.</p><p>6. The high concentrations required for some D-1 and D-2 agents to be effective, suggest an only partial consistency with mammalian dopaminergic receptors.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 297-301"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90211-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136596945","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90187-P
Fred Punzo
1. The effects of temperature on the topical toxicity of cypermethrin and fenvalerate to fifth-instar larvae of the fall annyworm, Spodoptera frugiperda, were investigated, as well as their effects on ataxia and prostration. Activities of carboxylesterase and glutathione S-transferase were also assessed.
2. Pyrethroid toxicities were characterized by a negative temperature coefficient (TC) between 15 and 27°C, and a positive TC between 27 and 38°C. Fenvalerate was more toxic at all test temperatures.
3. The median time for the onset of ataxia and prostration decreased as temperature increased.
4. Activity (μmol/min/mg protein) of carboxylesterase and glutathione S-transferase was significantly lower for fenvalerate-treated insects (217.4 and 17.2, respectively) than for cypermethrin (344.7, 39.7).
{"title":"Detoxification enzymes and the effects of temperature on the toxicity of pyrethroids to the fall armyworm, Spodoptera frugiperda (Lepidoptera:Noctuidae)","authors":"Fred Punzo","doi":"10.1016/0742-8413(93)90187-P","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90187-P","url":null,"abstract":"<div><p>1. The effects of temperature on the topical toxicity of cypermethrin and fenvalerate to fifth-instar larvae of the fall annyworm, <em>Spodoptera frugiperda</em>, were investigated, as well as their effects on ataxia and prostration. Activities of carboxylesterase and glutathione <em>S</em>-transferase were also assessed.</p><p>2. Pyrethroid toxicities were characterized by a negative temperature coefficient (TC) between 15 and 27°C, and a positive TC between 27 and 38°C. Fenvalerate was more toxic at all test temperatures.</p><p>3. The median time for the onset of ataxia and prostration decreased as temperature increased.</p><p>4. Activity (μmol/min/mg protein) of carboxylesterase and glutathione <em>S</em>-transferase was significantly lower for fenvalerate-treated insects (217.4 and 17.2, respectively) than for cypermethrin (344.7, 39.7).</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 155-158"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90187-P","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136598137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90201-U
Charles L. McKenney Jr , David M. Celestial
1. Exposure of the estuarine shrimp, Palaemonetes pugio, to a juvenile hormone analogue (⩾8 μg methoprene 1−1) throughout larval development inhibited successful completion of metamorphosis.
2. Methoprene exposure retarded growth in early larval stages and postlarvae, but enhanced growth in premetamorphic larvae.
3. Respiration rates of early larvae were elevated by methoprene exposure, but not so older larvae or post larvae.
4. Lower net growth efficiency (K2 values) in methoprene-exposed early larvae suggests that increased metabolic demands reduced assimilated energy available for growth.
5. Modifications in O:N ratios of premetamorphic larvae and postlarvae suggest that methoprene altered substrate utilization patterns during metamorphosis.
{"title":"Variations in larval growth and metabolism of an estuarine shrimp Palaemonetes pugio during toxicosis by an insect growth regulator","authors":"Charles L. McKenney Jr , David M. Celestial","doi":"10.1016/0742-8413(93)90201-U","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90201-U","url":null,"abstract":"<div><p>1. Exposure of the estuarine shrimp, <em>Palaemonetes pugio</em>, to a juvenile hormone analogue (⩾8 <em>μ</em>g methoprene 1<sup>−1</sup>) throughout larval development inhibited successful completion of metamorphosis.</p><p>2. Methoprene exposure retarded growth in early larval stages and postlarvae, but enhanced growth in premetamorphic larvae.</p><p>3. Respiration rates of early larvae were elevated by methoprene exposure, but not so older larvae or post larvae.</p><p>4. Lower net growth efficiency (<em>K</em><sub>2</sub> values) in methoprene-exposed early larvae suggests that increased metabolic demands reduced assimilated energy available for growth.</p><p>5. Modifications in O:N ratios of premetamorphic larvae and postlarvae suggest that methoprene altered substrate utilization patterns during metamorphosis.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 239-245"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90201-U","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597560","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1993-06-01DOI: 10.1016/0742-8413(93)90207-2
Izuru Kakuta, Shiro Murachi
1. Hb, MCHC, Na, Ca, Mg and Cu in plasma decreased with atypical Aeromonas salmonicida infection. Whilst plasma K and NPN increased.
2. Plasma Fe decreased markedly with infection. No statistically significant change in UIBC was found, though moribund eels showed slightly lower values compared to that of the control. The rate of decrease in TIBC is similar to that in most elements in plasma.
3. Fe content in most tissues decreased with infection. It increased in the gills and head muscle (infection site). No significant change was found in the intestine.
4. Water content in various tissues increased with infection.
{"title":"Changes of iron content in eels (Anguilla japonica) infected with atypical Aeromonas salmonicida","authors":"Izuru Kakuta, Shiro Murachi","doi":"10.1016/0742-8413(93)90207-2","DOIUrl":"https://doi.org/10.1016/0742-8413(93)90207-2","url":null,"abstract":"<div><p>1. Hb, MCHC, Na, Ca, Mg and Cu in plasma decreased with atypical <em>Aeromonas salmonicida</em> infection. Whilst plasma K and NPN increased.</p><p>2. Plasma Fe decreased markedly with infection. No statistically significant change in UIBC was found, though moribund eels showed slightly lower values compared to that of the control. The rate of decrease in TIBC is similar to that in most elements in plasma.</p><p>3. Fe content in most tissues decreased with infection. It increased in the gills and head muscle (infection site). No significant change was found in the intestine.</p><p>4. Water content in various tissues increased with infection.</p></div>","PeriodicalId":72650,"journal":{"name":"Comparative biochemistry and physiology. C: Comparative pharmacology","volume":"105 2","pages":"Pages 275-278"},"PeriodicalIF":0.0,"publicationDate":"1993-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0742-8413(93)90207-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136597557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}