Insect Biochemistry最新文献_第2页

Post-feeding induction of trypsin in the midgut of Aedes aegypti L. (Diptera: Culicidae) is separable into two cellular phases 进食后胰蛋白酶在埃及伊蚊(双翅目:库蚊科)中肠的诱导可分为两个细胞阶段

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90050-O

C.R. Felix , B. Betschart, P.F. Billingsley, T.A. Freyvogel

{"title":"Post-feeding induction of trypsin in the midgut of Aedes aegypti L. (Diptera: Culicidae) is separable into two cellular phases","authors":"C.R. Felix , B. Betschart, P.F. Billingsley, T.A. Freyvogel","doi":"10.1016/0020-1790(91)90050-O","DOIUrl":"10.1016/0020-1790(91)90050-O","url":null,"abstract":"<div>The induction of trypsin activity in the midgut of the mosquito, Aedes aegypti, was studied following meals of chicken blood, and several protein and peptide diets. Various concentrations of bovine serum albumin (BSA) in 0.15 M NaCl stimulated trypsin activity, in a similar fashion to the initial increase observed after a normal blood meal. Trypsin synthesis was also initiated when Ae. aegypti were fed on glutaraldehyde cross-linked BSA and on BSA fragments prepared by both pepsin and cyanogen bromide cleavage. Non-soluble proteins, in the form of glutaraldehyde-fixed erythrocyte ghosts, induced a delayed and reduced trypsin response, whilst small peptides from neutralized liver digests did not induce trypsin activity until 8–10 h after feeding. Metabolic inhibitors had varying effects on the post-feeding activity of trypsin stimulated by BSA feeding. Cycloheximide, a peptidyl transferase inhibitor prevented expression of all activity in vivo, whereas α-amanitin (RNA-polymerase inhibitor) did not affect trypsin activity in the first 10 h after feeding. At 20 μg/ml concentration in the diet, actinomycin D (RNA synthesis inhibitor) caused temporary superinduction followed by inhibition of trypsin activity, but at lower concentrations, the later phase of trypsin activity was inhibited. The results suggest that post-feeding induction of trypsin activity in Ae. aegypti is a two-phase process regulated at the midgut cellular level. The first phase of trypsin synthesis is stimulated by soluble proteins of variable molecular weights, and only involves translation of messenger RNA already available within the midgut cells. The second phase is stimulated by small peptides and requires complete synthesis of new mRNA from DNA.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 2","pages":"Pages 197-203"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90050-O","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79642708","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}

引用次数: 77

Adipokinetic hormone is dependent on extracellular Ca2+ for its stimulatory action on the glycogenolytic pathway in locust fat body in vitro 脂肪动力学激素依赖于细胞外Ca2+刺激刺槐脂肪体糖原溶解途径

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90003-W

W.J.A. Van Marrewijk, A.Th.M. Van den Broek, A.M.Th. Beenakkers

{"title":"Adipokinetic hormone is dependent on extracellular Ca2+ for its stimulatory action on the glycogenolytic pathway in locust fat body in vitro","authors":"W.J.A. Van Marrewijk, A.Th.M. Van den Broek, A.M.Th. Beenakkers","doi":"10.1016/0020-1790(91)90003-W","DOIUrl":"10.1016/0020-1790(91)90003-W","url":null,"abstract":"<div>Inclusion of glucose or trehalose in the medium during the incubation of locust fat body in vitro leads to a reduction of the relative amount of active (AMP-independent) glycogen phosphorylase. The presence of adipokinetic hormone (AKH I) results in a rapid activation of phosphorylase, reaching a maximum within 5 min. This AKH effect is highly dependent on added Ca2+, and requires ⩾ 1 mM Ca2+ for maximal enzyme activation. Ca2+ alone has no effect on phosphorylase activity, but it does activate the enzyme when the ionophore A23187 is also included in the medium. In a cell-free system from locust fat body the activation of endogenous phosphorylase by phosphorylase kinase is stimulated by Ca2+. Activity of the latter enzyme can be increased further by high doses of calmodulin. Both in the presence and in the absence of external calmodulin, the calmodulin antagonist trifluoperazine has an inhibitory effect on phosphorylase kinase. Results are discussed in relation to the possible mechanisms underlying hormonal control of glycogenolysis.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 4","pages":"Pages 375-380"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90003-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91097886","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}

引用次数: 39

Epoxide hydrolase activities in Drosophila melanogaster 黑腹果蝇环氧化物水解酶活性

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90095-V

L.G. Harshman , J. Casas , E.C. Dietze , B.D. Hammock

引用次数: 22

Cyanoprotein: Quantitative changes and synthesis in diapause and juvenile hormone analog treated bean bug, Riptortus clavatus 青色蛋白:滞育和幼期激素类似物处理后的豆虫数量变化和合成

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90110-Z

Ken Miura , Yasuo Chinzei , Tetsuro Shinoda , Hideharu Numata

{"title":"Cyanoprotein: Quantitative changes and synthesis in diapause and juvenile hormone analog treated bean bug, Riptortus clavatus","authors":"Ken Miura , Yasuo Chinzei , Tetsuro Shinoda , Hideharu Numata","doi":"10.1016/0020-1790(91)90110-Z","DOIUrl":"10.1016/0020-1790(91)90110-Z","url":null,"abstract":"<div>Quantitative changes of cyanoproteins (CPs) in diapause and juvenile hormone (JH) analog treated bean bug, Riptortus clavatus, were analyzed by rocket immunoelectrophoresis (RIE). In diapause-oriented nymphal females and males, CP-A (CP-1, 2 and 3) and CP-B (CP-4) increased and reached a maximum level just before nymphal-adult ecdysis, which was the same in non-diapause female and male nymphs. Both CP-A and B disappeared immediately after adult emergence. After this initial decline CP-4 appeared again in the hemolymph, followed after a few days by CP-1, 2 and 3. CP-A and B then increased slowly but constantly in both diapause female and male adults. Both diapause females and males at day 30 after adult emergence had large amounts of CP-A (CP-1, 2 and 3) and CP-B (CP-4). Treatment of diapause females (day 30) with methoprene induced only CP-1 synthesis and increased CP-A content about twice in both the whole body and the hemolymph, but did not effect on CP-B content. Methoprene treated females developed ovaries which accumulated yolk containing CPegg and vitellin (Vn). In diapause males treated with methoprene CP-A and B were not induced and decreased gradully in concentration, eventually disappearing completely, similar to post-diapause males (30 days after transferred to long day condition) in which CPs were not detected. These results show that methoprene treatment of diapause females and males induced the same dynamical situations of CP-A and B seen in non-diapause adults, i.e. only CP-A was induced in females and CPs disappeared in males. This suggests that CP synthesis is regulated by juvenile hormone.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 553-562"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90110-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75556357","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}

引用次数: 24

Cyclic AMP and calcium modulated ATPase activity in the salivary glands of the lone star tick Amblyomma americanum (L.) 环磷酸腺苷和钙对美国双星蜱唾液腺atp酶活性的调节

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90006-Z

Altaf E. Qureshi , Craig W. Roddy , Rebecca A. Mumma , Richard C. Essenberg , John R. Sauer

{"title":"Cyclic AMP and calcium modulated ATPase activity in the salivary glands of the lone star tick Amblyomma americanum (L.)","authors":"Altaf E. Qureshi , Craig W. Roddy , Rebecca A. Mumma , Richard C. Essenberg , John R. Sauer","doi":"10.1016/0020-1790(91)90006-Z","DOIUrl":"10.1016/0020-1790(91)90006-Z","url":null,"abstract":"<div>Na+,K+-activated ATPase activity in tick salivary glands increases during the rapid stage of tick feeding paralleling similar increases in dopamine and cAMP-stimulated fluid secretion. High concentrations of cyclic AMP increase Na+,K+-ATPase activity in a plasma membrane-enriched fraction from the salivary glands of rapidly feeding ticks. Cyclic AMP-dependent protein kinase inhibitor protein blocks activation of Na+,K+-ATPase activity at low but not high concentrations of cAMP indicating that both activator and inhibitor modulator phosphoproteins of Na+,K+-ATPase activity exist in the plasma membrane-enriched fraction.ATPase activity in the plasma membrane-enriched fraction is not measurable in the absence of Mg2+, Ca2+ and Na+. Ca-stimulated nucleotidase activity is highest with ATP serving as the preferred substrate in a series including CTP, UTP, GTP and ADP. Calcium, Mg2+ stimulated ATPase activity is activated further by calmodulin and partially inhibited by low concentration of vanadate, trifluoperazine and oligomycin. Results suggest that the plasma membrane-enriched fraction of tick salivary glands contains both Ca2+-ATPase activity and oligomycin-sensitive Ca2+, Mg2+-ATPase activities, the latter likely from a small amount of mitochondria in the partially purified organelle fraction.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 4","pages":"Pages 399-405"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90006-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74924197","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}

引用次数: 3

Dietary ascorbic acid, pyridoxine and riboflavin reduce the light sensitivity of larvae and pupae of Drosophila melanogaster 饲粮中添加抗坏血酸、吡哆醇和核黄素可降低黑腹果蝇幼虫和蛹的光敏性

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90108-Q

B.G. Bruins, W. Scharloo, G.E.W. Thörig

{"title":"Dietary ascorbic acid, pyridoxine and riboflavin reduce the light sensitivity of larvae and pupae of Drosophila melanogaster","authors":"B.G. Bruins, W. Scharloo, G.E.W. Thörig","doi":"10.1016/0020-1790(91)90108-Q","DOIUrl":"10.1016/0020-1790(91)90108-Q","url":null,"abstract":"<div>Drosophilia melanogaster is light sensitive. On low yeast media, light induces high mortality during the development from egg to adulthood and increases development time. This effect of light is strongly dependent on the yeast-concentration. Addition of 8 vitamins, normally present in yeast, protects Drosophila against light under laboratory conditions. In this study we have analyzed the significance of the individual vitamins for both survival and development at high light intensities. Two D. melanogaster strains were utilized: a control strain C and a strain P. The latter had been adapted to a palmitic acid supplemented medium. In addition, we investigated the effect of vitamin C, a vitamin typically found in fruit, but not in yeast. It appears that both pyridoxine and riboflavin are essential for the survival of the control strain C under high light intensities, and they act synergistically. The other 6 tested vitamins can be omitted in these survival experiments. Moreover survival under high light conditions also improved strongly on media supplemented with vitamin C. The other strain (P), which was for many generations kept on a different food-medium, also was protected on yeast media by riboflavin and pyridoxine, and by vitamin C, although the survival at high light intensities on media with riboflavin and pyridoxine was less than the survival of the control strain.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 541-544"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90108-Q","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74698514","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}

引用次数: 5

Studies on the subcellular distribution of (Na+ + K+)-ATPase, K+-stimulated ATPase and HCO3−-stimulated ATPase activities in malpighian tubules of Locusta migratoria L. （Na++K+）-ATP酶、K+刺激ATP酶和HCO3刺激ATP酶活性在飞蝗马氏小管亚细胞分布的研究。

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90116-V

K.E. Fogg, J.H. Anstee, D. Hyde

引用次数: 31

Characterization of hemolymph juvenile hormone esterase from Lymantria dispar 野毒蛾血淋巴幼激素酯酶的研究

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90028-D

Algimantas P. Valaitis

{"title":"Characterization of hemolymph juvenile hormone esterase from Lymantria dispar","authors":"Algimantas P. Valaitis","doi":"10.1016/0020-1790(91)90028-D","DOIUrl":"10.1016/0020-1790(91)90028-D","url":null,"abstract":"<div>A major peak of juvenile hormone esterase (JHE) activity approaching 330 nmol JH III hydrolyzed/min/ml of hemolymph was observed during the last larval growth stage in Lymantria dispar. A smaller peak of JHE occurred 3–5 days after pupation. The gypsy moth JHE was purified from larval hemolymph using a classical approach. A specific activity of 766 units per mg of protein and a Km of 3.6 × 10−7 M for racemic JH III and the (10R, 11S) enantiomer of JH II was determined for the purified enzyme. The 62 kDa esterase was insensitive to inhibition by O,O-diisopropyl phosphorofluoridate (DFP), or by phenylmethylsulfonyl fluoride (PMSF). Two forms of JHE isolated by RP-HPLC were indistinguishable by HPLC tryptic peptide mapping and share an identical N-terminal amino acid sequence. Polyclonal antisera raised against gypsy moth enzyme cross-reacted with JHE from Trichoplusia ni but not with JHE from Manduca sexta. A weak cross-reactivity was observed with JHE from Heliothis virescens. Forty amino acid residues of the N-terminus were placed in sequence. The N-terminal sequence of JHE from L. dispar showed little homology to the sequence of JHE from H. virescens. The immunological and structural data support the conclusion that markedly different esterases, which catalyze the hydrolysis of juvenile hormone, are present in the hemolymph of different Lepidoptera.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 6","pages":"Pages 583-595"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90028-D","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79087652","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}

引用次数: 18

Characterization of the ATP:2-deoxyecdysone 22-phosphotransferase (2-deoxyecdysone 22-kinase) in the follicle cells of Schistocerca gregaria 日本血吸虫卵泡细胞ATP:2-脱氧脱皮激素22-磷酸转移酶(2-脱氧脱皮激素22-激酶)的研究

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90064-L

Mohamed Kabbouh, Huw H. Rees

{"title":"Characterization of the ATP:2-deoxyecdysone 22-phosphotransferase (2-deoxyecdysone 22-kinase) in the follicle cells of Schistocerca gregaria","authors":"Mohamed Kabbouh, Huw H. Rees","doi":"10.1016/0020-1790(91)90064-L","DOIUrl":"10.1016/0020-1790(91)90064-L","url":null,"abstract":"<div>Follicle cells were isolated from their oocytes using 0.15% collagenase and low speed centrifugation. Incubation of the follicle cell pellet with [3H]2-deoxyecdysone yielded its 22-phosphate ester conjugate. Addition of ATP/Mg2+ or GTP/Mg2+ to follicle cell homogenate incubated with 2-deoxyecdysone increased the phosphotransferase activity by 4-fold for ATP and 2-fold for GTP. In the case of intact cells, only ATP was effective. The enzyme had a cytosolic subcellular localization and its <math><mtext>K</mtext><msub><mi></mi><mn><mtext>m</mtext></mn></msub></math> for 2-deoxyecdysone was 3 μM. The phosphotransferase activity required the presence of both ATP and Mg2+, and had an apparent <math><mtext>K</mtext><msub><mi></mi><mn><mtext>m</mtext></mn></msub></math> for ATP of 0.83 mM, with maximum activity being obtained in the presence of 10 mM Mg2+. The activity was strongly inhibited in the presence of Ca2+ with <math><mtext>IC</mtext><msub><mi></mi><mn>50</mn></msub><mtext> = 1</mtext></math> mM. The reaction rate was linear for 10 min and with increasing protein concentrations up to 1 mg/ml. Optimal pH was about 7.4 and the optimal temperature was 37°C. The phosphotransferase activity survived freezing at −20°C, but was totally abolished by heat at 60°C for 10 min. Investigation of the variation in activity of the phosphotransferase during ovarian development revealed a peak at the end of oogenesis in excellent agreement with the titre of ecdysteroid 22-phosphates found in the oocytes just before chorionation and egg-laying.</div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 1","pages":"Pages 57-64"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90064-L","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81713357","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}

引用次数: 11

Purine interconversions in the Australian termite, Nasutitermes walkeri hill 澳洲白蚁的嘌呤相互转化

Insect Biochemistry Pub Date : 1991-01-01 DOI: 10.1016/0020-1790(91)90007-2

D.J. Chappell, M. Slaytor

引用次数: 5