Insect Biochemistry最新文献

{"title":"Sequences of two cDNAs and expression of the genes encoding methionine-rich storage proteins of Manduca sexta","authors":"Lolita M. Corpuz ,&nbsp;Hee Choi ,&nbsp;S. Muthukrishnan ,&nbsp;Karl J. Kramer","doi":"10.1016/0020-1790(91)90016-8","DOIUrl":"10.1016/0020-1790(91)90016-8","url":null,"abstract":"<div><p>In <em>Manduca sexta</em>, storage proteins accumulate during the final larval stadium for utilization during subsequent larval-pupal-adult transformations. Two cDNA clones (designated clone 119 and clone 201), that represent two distinct but related genes (42% sequence identity), were isolated from a cDNA library prepared from day 7 fifth instar larval fat body and found to encode two different storage proteins synthesized during the last larval instar. Northern blot analyses revealed that the two clones hybridize to 2.4 kb transcripts that are translated to 79 kDa protein products during <em>in vitro</em> translation experiments. Clone 119 encodes a methionine-rich storage protein, designated as SP1A, that shares 37% sequence identity with the <em>Bombyx mori</em> sex-specific storage protein SP1. Clone 201, on the other hand encodes a storage protein, designated as SP1B, that is more closely related to <em>B. mori</em> SP1 (63% identity), and is probably identical to the <em>Manduca</em> female-specific storage protein (FSP). Insert DNA from clone 201, but not clone 119, cross-hybridizes to that of FSP cDNA (Webb and Riddiford, <em>Dev. Biol.</em><strong>130,</strong> 671–691, 1988a). Both storage proteins are synthesized only in the fat body and only during the fifth larval stadium, indicating tissue- and stage-specific expression of the two genes. Both genes exhibit sex-specific differences in expression. In the fifth larval stadium, the mRNAs for the SP1A and SP1B proteins begin to accumulate at about day 2 in the female fat body but appear 2 or 3 days later in the male fat body. In both sexes SP1A mRNA remains relatively high beyond the time when SP1B mRNA has already declined to low levels, suggesting differences in mRNA stability or expression. Injection of 20-hydroxyecdysone into ligated fifth instar abdomens causes substantial increases in the levels of both mRNAs, whereas topical application of the juvenile hormone mimc, fenoxycarb, to feeding fifth instar larvae produces substantial declines in the mRNA levels, indicating hormonal effects at the transcriptional level. The data support the hypothesis that the expression of these <em>M. sexta</em> methionine-rich storage protein genes is stimulated by ecdysteroid and inhibited by juvenile hormone.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 265-276"},"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)90016-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84745673","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}

{"title":"cDNA and deduced amino acid sequence of a blood meal-induced trypsin from the mosquito, Aedes aegypti","authors":"Carolina Barillas-Mury ,&nbsp;Rolf Graf ,&nbsp;Henry H. Hagedorn ,&nbsp;Michael A. Wells","doi":"10.1016/0020-1790(91)90089-W","DOIUrl":"10.1016/0020-1790(91)90089-W","url":null,"abstract":"<div><p>A cDNA for a midgut trypsin induced by a blood meal has been cloned and sequenced from the mosquito <em>Aedes aegypti</em>. The 862 base sequence codes for a 257 amino acid protein, which is presumably a trypsin precursor, since the sequence of purified mosquito trypsin begins at residue 26, immediately following an arginine residue in the precursor. The amino terminal 25 amino acids in the precursor are composed of a putative 15 amino acid signal peptide and a 10 amino acid activation peptide. Compared to vertebrate trypsinogens, the putative mosquito trysinogen lacks the four acidic amino acids immediately preceding the basic amino acid at the activation peptide cleavage site, suggesting the mechanism of its activation may be different from the activation of vertebrate trypsinogens. However, since a trypsinogen has not yet been isolated from the mosquito, these conclusions are tentative. The deduced amino acid sequence is homologous to that of other trypsins in those residues around the catalytic triad, and in several residues which are found only in trypsins. However, the sequence of the specificity pocket in mosquito trypsin, KESPC, differs from that found in other trypins, KDSC. The Asp is thought to bind the basic residue of the substrate, and the Glu in the mosquito trypsin may serve the same role. The changes in trypsin protein and mRNA levels following a blood meal indicate that an important component of the regulation of trypsin synthesis is at the transcriptional level.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 8","pages":"Pages 825-831"},"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)90089-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91248144","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}

{"title":"Glutathione S-transferase activities in phytophagous insects: Induction and inhibition by plant phototoxins and phenols","authors":"Keywan Lee","doi":"10.1016/0020-1790(91)90001-U","DOIUrl":"10.1016/0020-1790(91)90001-U","url":null,"abstract":"<div><p>The effects of two plant phototoxins (xanthotoxin and harmine) and three plant phenols (quercetin, ellagic acid, and juglone) on detoxification enzymes were studied in the polyphagous cabbage looper, <em>Trichoplusia ni</em>, and the oligophagous black swallowtail, <em>Papilio polyxenes</em>. In <em>P. polyxenes</em>, glutathione <em>S</em>-transferase (GST) activities toward 1-chloro-2,4-dinitrobenzene (CDNB) were 1840 and 1750 nmol CDNB conjugate/mg protein/min in the cytosolic fraction of midgut and fat body, respectively. Dietary xanthotoxin (0.1% fw) increased the activity 2.5 and 2.9-fold in the midgut and fat body, respectively. Xanthotoxin-conjugating GST activity was absent in both tissues. In <em>T. ni</em>, GST activity, 513 nmol CDNB conjugate/mg protein/min in the cytosolic fraction of midgut, was increased almost twofold by dietary xanthotoxin and harmine. Plant phenols effectively inhibited <em>in vitro</em> GST and Se-independent glutathione peroxidase (GPOX) activities in a dose-dependent manner in the two species. Both GST and GPOX of <em>P. polyxenes</em> were 2-fold less sensitive to phenol inhibitors than <em>T. ni</em>. GST inhibition differed according to the nature of the inhibitor in <em>P. polyxenes</em>. Quercetin is competitive with CDNB and is non-competitive with respect to GSH. In contrast, inhibition by ellagic acid is non-competitive with CDNB and competitive with GSH. Juglone showed competitive inhibition with both GSH and CDNB.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 4","pages":"Pages 353-361"},"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)90001-U","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78923083","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}

{"title":"Changes in the hemolymph lipophorin and very high density lipoprotein levels during the fifth nymphal and adult stages of Triatoma infestans","authors":"María S. González,&nbsp;JoséLuis Soulages,&nbsp;Rodolfo R. Brenner","doi":"10.1016/0020-1790(91)90038-G","DOIUrl":"10.1016/0020-1790(91)90038-G","url":null,"abstract":"<div><p>The occurrence of lipophorin (HDLp) and a very high density lipoprotein (VHDL) throughout the last nymphal and adult stages of male <em>T. infestans</em> was followed by quantitative immunodiffusion using specific antisera derived from the purified lipoproteins of adult male insects. Significant changes on the concentration of these hemolymph lipoproteins (Lps) occurred during the mentioned developmental stages. These changes include the following. A great accumulation of hemolymph proteins and Lps, particularly VHDL, during the nymphal stage. This increase reached a peak just before the last molt, where the concentration of VHDL and HDLp were 74 and 42 mg/ml hemolymph, respectively. A sharp decline in the Lps concentration just after the molt and during the first 2 weeks of adult life. These changes imply a six-fold decrease on the VHDL and a two-fold decrease in the HDLp concentrations. Another increase in the protein concentration that begins around the third week of the adult stage affecting both Lps, but mainly the HDLp. From its hexameric structure, amino acid composition and high concentration in nymphal stages, the VHDL of <em>T. infestans</em> could be considered a storage protein. The fact that VHDL persists in a considerable concentration in the hemolymph of adult insects differenciates this VHDL from this protein. The distribution of ¹⁴C free fatty acid (FFA) among the hemolymph proteins of <em>T. infestans</em> shows that the FFA are associated only with VHDL and HDLp. The developmental changes of the Lps pattern are accompanied by changes in the relative distribution of FFA between these Lps. The VHDL is the principal carrier of FFA during the fifth-nymph stage while HDLp is the main protein and FFA-carrier in adult life.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 6","pages":"Pages 679-687"},"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)90038-G","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73555007","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}

{"title":"Properties of glycosidases from the maize weevil, Sitophilus zeamais","authors":"J.E. Baker","doi":"10.1016/0020-1790(91)90031-9","DOIUrl":"10.1016/0020-1790(91)90031-9","url":null,"abstract":"<div><p>A survey of glycosidase activity in adults of the maize weevil, <em>Sitophilus zeamais</em> Motschulsky, indicated a complex of enzymes qualitatively sufficient to hydrolyze the free di- and oligosaccharides in their cereal diets as well as the maltose and oligomaltodextrins produced by the action of α-amylase on ingested starch. Glycosidase activity was found primarily in the soluble fraction (105,000 <em>g</em> supernatant) of gut (foregut, midgut and contents) homogenates and was most active in buffers with slightly acidic pH. α-Glucosidase activity was detected by using <span><math><mtext>p-</mtext><mtext>nitrophenyl</mtext><mtext>-α-</mtext><mtext>d</mtext><mtext>-glucopyranoside</mtext></math></span> (NPαGlu), maltose, sucrose and melezitose as substrates. Based on differences in pH optima, there may be a specific α-trehalase. β-Glucosidase activity was detected with <span><math><mtext>p-</mtext><mtext>nitrophenyl</mtext><mtext>-β-</mtext><mtext>d</mtext><mtext>-glucopyranoside</mtext></math></span> and cellobiose. <span><math><mtext>p-</mtext><mtext>Nitrophenyl</mtext><mtext>-α-</mtext><mtext>d</mtext><mtext>-galactopyranoside</mtext></math></span> was not hydrolyzed but the slow hydrolysis of melibiose indicated the presence of an α-galactosidase. β-Galactosidase was detected with <span><math><mtext>p-</mtext><mtext>nitrophenyl</mtext><mtext>-β-</mtext><mtext>d</mtext><mtext>-galactopyranoside</mtext></math></span>. Raffinose was slowly hydrolyzed. The molecular mass of α-glucosidase, partially purified from adult weevils by ammonium sulfate precipitation and ion exchange chromatography, was estimated to be 130 kDa under non-dissociating conditions. α-Glucosidase activity was detected at <em>R</em>_m 0.43 on 7.5% acrylamide gels with 4-methyl-umbelliferyl-α-<span>d</span>-glucoside as substrate. pI was estimated to be 4.9 by isoelectric focusing. Two fractions with activity against <span><math><mtext>p-</mtext><mtext>nitrophenyl</mtext><mtext>-α-</mtext><mtext>d</mtext><mtext>-glucopyranoside</mtext></math></span> were resolved by high performance liquid chromatography. One fraction (peak No. 2) was highly specific for maltose, had <em>K</em>_m values of 12.9 mM for NPαGlu and 14 mM for maltose, and hydrolyzed oligomaltodextrins up to at least maltoheptaose</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 6","pages":"Pages 615-621"},"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)90031-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90162607","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}

{"title":"Alkaline phosphatase from the excretory system of the grasshopper, Poekilocerus bufonius","authors":"Samir M. Khoja","doi":"10.1016/0020-1790(91)90012-4","DOIUrl":"10.1016/0020-1790(91)90012-4","url":null,"abstract":"<div><p>Alkaline phosphatase from the excretory system of the grasshopper, <em>Poekilocerus bufonius</em> was purified with ammonium sulphate fractionation and chromatography on Bio-Gel A-0.5 m. The specific activity of the enzyme is 152 units/mg of protein. The enzyme is a tetramer and the <em>M</em>_r value of the subunit is 72,000 ± 2500 as shown by gel filtration and SDS-polyacrylamide gel electrophoresis. The enzyme has a pH optimum of 9.6 and an apparent <em>K</em>_m value of 0.28 × 10⁻³ M. The activity of the enzyme reached a maximum at 75°C and the enzyme showed stability at 65°C. The enzyme was inhibited by Ca²⁺, Na⁺ and Fe³⁺ and was stimulated by Zn²⁺, Mn²⁺ and Mg²⁺.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 239-242"},"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)90012-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77219052","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}

{"title":"Isolation, identification and synthesis of Lom-AG-myotropin II, a novel peptide in the male accessory reproductive glands of Locusta migratoria","authors":"L. Paemen ,&nbsp;L. Schoofs ,&nbsp;P. Proost ,&nbsp;B. Decock ,&nbsp;A. De Loof","doi":"10.1016/0020-1790(91)90013-5","DOIUrl":"10.1016/0020-1790(91)90013-5","url":null,"abstract":"<div><p>The male accessory glands of <em>Locusta</em> contain factors which stimulate oviduct contraction. From an extract of 4400 gland masses, a myotropic peptide (Lom-AG-myotropin II) was isolated by HPLC. Sequencing revealed the following sequence: Ala-His-Arg-Phe-Ala-Ala-Glu-Asp-Phe-Gly-Ala-Leu-Asp-Thr-Ala. Chemical synthesis confirmed that this peptide is active in the acid form instead of the amide form as other presently known myotropic peptides. The sequence does not resemble that of any peptide isolated from <em>Locusta</em> or other insects. The myotropin is active on the oviduct of <em>Locusta migratoria</em> but not on the oviduct of <em>Leucophaea maderae</em>. The myotropic activity can be detected on the hindgut of both insects but at much higher peptide concentrations.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 243-248"},"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)90013-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81600299","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}

{"title":"Evolution of glutathione S-transferase subunits in culicidae and related nematocera: Electrophoretic and immunological evidence for conserved enzyme structure and expression","authors":"David F. Grant","doi":"10.1016/0020-1790(91)90010-C","DOIUrl":"10.1016/0020-1790(91)90010-C","url":null,"abstract":"<div><p>The antigenic relatedness and molecular weights of glutathione <em>S</em>-transferase (GST) protein subunits expressed by representative members of the Dipteran suborder Nematocera were analyzed by immunoblotting and affinity chromatography. Ten species within the genus <em>Aedes</em> expressed two subunits which cross-reacted with an antiserum developed against the GST-1b isozyme purified from <em>Aedes aegypti</em>. One of these two subunits showed no discernible molecular weight variability within the ten <em>Aedes</em> species. Its molecular weight (25,900 Da) was identical to the GST-1a subunit found in <em>A. aegypti</em>. The molecular weight of the other subunits varied among the ten species, but in all cases was larger than 25,900 Da. In ten species within the genus <em>Anopheles</em> (considered to be among the more primitive genera in the Culicidae), only one immunologically related GST subunit was expressed. Its molecular weight was also identical to the GST-1a subunit found in the <em>Aedes</em> species. Members of genera considered phylogenetically intermediate between <em>Anopheles</em> and <em>Aedes</em> had either one or two cross-reacting subunits. Representative species of families closely related to the Culicidae (the Chaoboridae, Chironomidae, Simuliidae, and Cecidomyiidae) also expressed immunologically related GST subunits. GST isozymes were partially purified from <em>Anopheles freeborni</em> and <em>A aegypti</em> adults, larvae, and ovaries using <em>S</em>-hexylglutathione affinity chromatography. Adult and larval <em>Anopheles freeborni</em> expressed not only the immunologically related subunit, but an additional, immunologically unrelated subunit. In fully developed ovaries of both species, however, only subunits immunologically related to GST-1b were expressed. These results suggest that there is an immunologically conserved domain shared among specific GST isozymes within the Nemotocea. The conserved nature of these GST subunits, their correlation with oocyte development, and their localization within ovary tissue, suggests that they share a conserved <em>in vivo</em> function during oocyte maturation. In addition, the conserved antibody binding domain within these subunits apparently has been duplicated in several species of Culicidae.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 4","pages":"Pages 435-445"},"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)90010-C","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84598906","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}

{"title":"Cuticle proteins of the boll weevil, Anthonomus grandis, abdomen: Structural similarities and glycosylation","authors":"Brad Stiles","doi":"10.1016/0020-1790(91)90014-6","DOIUrl":"10.1016/0020-1790(91)90014-6","url":null,"abstract":"<div><p>Cuticle proteins are thought to be important in defining the structural and functional differences occurring in insect cuticle. In order to explain and better understand the structural similarities among the cuticle proteins of the cotton boll weevil, <em>Anthonomus grandis</em> Boheman, described in a previous study (Stiles and Leopold, 1990, <em>Insect Biochem.</em><strong>20</strong>, 113–125) three series of monoclonal antibody producing hybridoma cell lines were produced. Larval, pupal or adult cuticle proteins were used as antigens. While some of the monoclonal antibodies were specific for one or two cuticle proteins from a single developmental stage, the majority showed multiple cuticle protein binding patterns on Western blots. To determine whether this cross-reaction was due to common oligosaccharide chains bound to the proteins, lectins were used to probe Western blots. Many of the cuticle proteins were found to be glycosylated. The majority of the Con A reactive carbohydrate could be removed from the protein by <em>N</em>-glycosidase F digestion (specific for <em>N</em>-asparagine linked carbohydrate). <em>N</em>-glycosidase F digestion did not reduce the multiple cross-reactions of the monoclonal antibodies, nor did periodate oxidation of the CP. The carbohydrate remaining after enzyme digestion is presumably <em>O</em>-linked to serine/threonine.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 249-258"},"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)90014-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86416185","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}

{"title":"Incorporation of arylphorins (LSP-1) and LSP-2 like protein into the integument of Ceratitis capitata during pupariation","authors":"Sotiris Tsakas,&nbsp;Panagiotis G. Katsoris,&nbsp;Kostas Bourtzis,&nbsp;Vassilis J. Marmaras","doi":"10.1016/0020-1790(91)90104-M","DOIUrl":"10.1016/0020-1790(91)90104-M","url":null,"abstract":"<div><p>The arylphorins and LSP-2 like polypeptide were detected by immunoblotting analysis during development in the integument of <em>C. capitata</em>. <em>In vitro</em> translation of total RNA from fat body and integument during pupariation, clearly revealed that the polypeptides under consideration were exclusively synthesized in the fat body. Furthermore, <em>in vitro</em> experiments demonstrated that radiolabeled arylphorins and LSP-2 like polypeptide were taken up by the integument, in an undegraded state. Immunofluorescence experiments in cross sections of wandering stage larvae and white pupae revealed that the LSP-2 like polypeptide was mainly localized in the epidermal cells, and a very weak signal was also given by the cuticle. Furthermore, the presented results indicated that a small portion of the extracted proteins exist in high molecular weight aggregate(s).</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 507-515"},"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)90104-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86136051","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}