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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (11)
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  • 1
    Electronic Resource
    Electronic Resource
    Preface (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 1-2 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030702
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  • 2
    Electronic Resource
    Electronic Resource
    Partial purification and characterization of phenobarbital-induced house fly cytochrome P-450 (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1983), S. 127-138 
    Details
    ISSN: 0739-4462
    Keywords: aldrin epoxidase ; column chromatography ; cytochrome P-450 ; house fly ; Musca domestica ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two forms of phenobarbital-induced cytochrome P-450 were partially purified from the Rutgers diazinon-resistant strain of house fly using cholate solubilization, polyethylene glycol 6000 precipitation, and chromatography on DEAE cellulose. The preparation of highest purity had an absorbance maximum of 452 nm, a specific content of 10.0 nmol/mg protein, and an apparent molecular weight of 60,000 when examined by sodium dodecyl sulfate polyacrylamide electrophoresis. The yield of the highly purified cytochrome P-450 was 2-3%. This form contained proportionately less cytochrome P-420 than the original cholate solubilized microsomes, and is thus apparently more stable. A second form of cytochrome P-450 having a specific content of 0.50-0.89 nmol/mg protein was eluted from DEAE cellulose with a 0-0.25 M salt gradient. This is consistent with a previously reported elution pattern for Emulgen 913-solubilized house fly microsomes. Several methods of solubilizing house fly microsomes were examined. High salt, 2M KCI, in the absence of detergents effectively solubilized cytochrome P-450 (50-70% recovery) with little or no conversion to cytochrome P-(420).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940010202
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  • 3
    Electronic Resource
    Electronic Resource
    Purification, characterization, and synthesis of vitellin from the cabbage butterfly Pieris rapae L. (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 67-79 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenin ; juvenile hormone ; immunoelectrophoresis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Vitellin from the cabbage butterfly Pieris rapae L. was purified and characterized by electrophoresis. Vitellin from P. rapae is a phosphorylated glycolipoprotein of 380,000 ± 10,000 molecular weight as determined by nondenaturing polyacrylamide gel electrophoresis. Two subunits with an Mr of 150,000 and 40,000 were obtained from vitellin. The native molecule is thought to be a tetramer composed of two molecules of each of these subunits. The isoelectric point, as determined by isoelectric focusing on polyacrylamide gels, is 6.10. Vitellin and vitellogenin were indistinguishable by immunological methods such as double diffusion and tandem-crossed immunoelectrophoresis. Vitellogenin from the hemolymph and vitellin from the ovary were quantified by rocket immunoelectrophoresis. Vitellogenin and vitellin were first detected in 6-day-old pupae, and their levels increased continuously during ovarian development. Vitellogenin synthesis by the fat body in 4-day-old female pupae could be induced by juvenile hormone I.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090105
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  • 4
    Electronic Resource
    Electronic Resource
    Membrane binding and uptake of diflubenzuron in a cell line from Manduca sexta (L.)This paper reports the results of research only. Mention of a pesticide in this paper does not constitute a recommendation by the U.S. Department of Agriculture nor does it imply registration under FIFRA. (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 169-182 
    Details
    ISSN: 0739-4462
    Keywords: insect growth regulators ; binding ; plasma membrane ; chitin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding and accumulation of the chitin synthesis inhibitor diflubenzuron (DFB) by a cell line derived from embryonic tissue of the tobacco hornworm, Manduca sexta (L.), was analyzed. A rapid and reversible binding to viable and nonviable cells suspended in the culture medium was observed at soluble concentrations of DFB for short exposure periods. Scatchard analysis gave no indication of a saturable uptake mechanism. The DFB-binding capacity of intact cells was found to be similar to that of a crude membrane preparation (70,000g pellet); however, plasma membrane-enriched fractions bound almost three times as much DFB as the homogenate. Repetitive shorttime incubations (up to 3 h) of suspended cells with DFB resulted in a stepwise intracellular accumulation of DFB. Treatment of growing cells with DFB at high concentrations (50 μM) of DFB for longer periods (up to 7 days) resulted in elevated intracellular accumulation of DFB, which exceeded the binding capacity of the cell membranes and the aqueous solubility of DFB. These results indicate that the intracellular crystals detected by transmission electron microscopy are precipitated DFB. No metabolites or other chemically modified products of intracellular DFB were detected by high pressure liquid chromatography (HPLC) after a 7-day incubation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940040303
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of mannosyl transferases during the pupal instar of Stomoxys calcitrans (L) (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1983), S. 1-15 
    Details
    ISSN: 0739-4462
    Keywords: Stomoxys calcitrans ; mannosyl transferase ; stable fly ; glycosyl transferase ; dolicholphosphate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Particulate fractions (10,000g) from pupae of Stomoxys calcitrans transfer [14C]-mannose from GDP-[14C]-mannose to dolichol monophosphate and proteins. Production of the mannosyl lipid was inhibited by Mn2+, UDP, GMP, GDP, and EDTA. The insect growth regulator diflubenzuron had no effect on mannosyl transferase activity. Dolichol monophosphate and Mg2+ stimulated mannosyl transferase activity. The mannosyl lipid product was identified as mannosyl-phosphoryl-dolichol (Man-P-Dol). The apparent Km and Vmax values for the formation of Man-P-Dol using GDP-[14C]-Man while holding dolichol phosphate constant were 2.4 ± 0.9 μM and 9.4 ± 2.3 pmol Man-P-Dol·min-1·mg-1 protein, respectively. The apparent Km and Vmax values using dólichol phosphate while holding GDP-Man constant were 2.2 ± 1.2 μM and 18.5 ± 1.7 pmol Man-P-Dol·min-1·mg-1 protein.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940010102
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  • 6
    Electronic Resource
    Electronic Resource
    Properties, synthesis, and accumulation of storage proteins in Pieris rapae L. (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 215-228 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph ; fat body ; storage granules ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two kinds of storage proteins (SP-1, SP-2) were confirmed in hemolymph and fat body of Pieris rapae during metamorphosis. Both proteins were present in high concentrations in the hemolymph during the last larval instar. Hemolymph concentrations of SP-1 and SP-2 dropped after pupation as the proteins were being deposited in fat bodies. SP-2 is present in a larger amount than SP-1. Detailed studies on storage proteins determined their properties, mode of synthesis, and accumulation in the fat body.SP-1 has a molecular weight of 500,000 and consists of one type of subunit (Mr 77,000), while SP-2 has a molecular weight of 460,000 and is composed of two types of subunits (Mr 80,000 and 69,000). The pl values of SP-1 and SP-2 were determined to be 6.97 and 7.06, respectively.Fat body cells from 1-day-old fifth instar larvae synthesized storage proteins in large amounts, whereas those from late prepupae exhibited high protein sequestration. Proteins taken up in fat body accumulated in dense granules during the pupal stage but sharply decreased at the adult stage.Morphological changes in the fat body tissues were observed during the larval-pupal transformation; the nuclei of fat body cells became irregularly shaped, and the boundaries between cells seemed to be obscure. Synthesis, storage, or degradation of storage proteins in fat body during development is closely associated with morphological changes in the tissues.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100305
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  • 7
    Electronic Resource
    Electronic Resource
    Gut chitin synthase and sterols from larvae of Diaprepes abbreviatus (Coleoptera: Curculionidae) (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 18 (1991), S. 105-117 
    Details
    ISSN: 0739-4462
    Keywords: chitin synthesis inhibitors ; ecdysteroids ; molting hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Gut chitin synthase was characterized and the sterols and ecdysteroids in the sugarcane rootstalk borer weevil, Diaprepes abbreviatus, were identified. An in vitro cell-free chitin synthase assay was developed using larval gut tissues from D. abbreviatus. Subcellular fractionation experiments showed that the majority of chitin synthase activity was located in 10,000g pellets. The gut chitin synthase requires Mg2+ to be fully active: 7-8-fold increases in activity were obtained with 10 mM Mg2+ present in reaction mixture. Calcium also stimulated activity (4-5-fold with 10 mM Ca2+), while Cu+2 completely inhibited at 1 mM. Other monovalent and divalent cations had little or no effect on activity. The pH and temperature optima were 7 and 25°C, respectively. Gut chitin synthesis was activated ca. 50% by trypsin treatments. GlcNAc stimulated chitin synthase activity, but Glc, GlcN and glycerin did not. Polyoxin D, UDP, and ADP inhibited the chitin synthase reaction with I50's of 75 μM, 2.3 mM, and 3.6 mM, respectively. Nikkomycin Z was a potent inhibitor of chitin synthase (91% inhibition at 10 μM). Tunicamycin and diflubenzuron had no effect on the enzyme. The apparent Km and Vmax for the gut chitin synthase were, respectively, 122.5 ± 7.4 μM and 426 ± 19.7 pmol/h/mg protein utilizing UDP-GlcNAc as the substrate. Sterol analyses indicated that cholesterol was the major dietary and larval sterol. HPLC/RIA data indicated that 20-hydroxyecdysone was the major molting hormone.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940180205
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  • 8
    Electronic Resource
    Electronic Resource
    N-acetylglucosaminyl transferases from the pupal instar of the stable fly, Stomoxys calcitrans (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 161-179 
    Details
    ISSN: 0739-4462
    Keywords: stable fly ; Stomoxys calcitrans ; N-acetylglucosaminyl transferases ; glycosyltransferases ; tunicamycin ; carbohydrate metabolism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: N-acetylglucosaminyl transferases from pupae of Stomoxys calcitrans (L.) were studied in 10,000g pellet suspensions. Characterization of these enzymes was based on formation of glycolipids (ie, Dol·PP-GlcNAc and Dol·PP-(GlcNAc)2), oligosaccharide lipids, and giycoproteins. Studies on transferase activity during the pupal instar showed that there were two peaks of activity; the first peak was on day 0 (prepupae) and the second at 3 days after pupation. Subcellular fractionation indicated that 10,000g and 100,000g pellets contained most of the transferase activities. The transferases required divalent cations (either Mn2+ or Mg2+). The pH optimum, which varied for each of the products formed, was 7.5 for glycolipids, 7.0 for oligosaccharide lipids, and 6.5 for glycoprotein. Inclusion of dolichol monophosphate doubled the amount of Dol·PP-GlcNAc and Dol·PP·(GlcNAc)2 formed, but had little effect on oligosaccharide lipid and glycoprotein formation.Tunicamycin was a potent inhibitor of glycolipid formation with an I50 of 1.8-4.8 nM. It was confirmed that tunicamycin acts by preventing the transfer of GlcNAc-1-P from UDP-GlcNAc to Dol·P. UMP reverses glycolipid formation, yielding UDP-GlcNAc. Some characterization of the products was performed. Glycolipids were shown to be Dol·PP-GlcNAc and Dol·PP-(GlcNAc)2. Glycoprotein was rapidly solubilized by protease and detergent treatments, whereas oligosaccharide lipids appeared to be acid-labile, pyrophosphate-containing lipids. The apparent kinetic constants for the formation of glycolipids were as follows: UDP-GlcNAc Km = 1.55 ± 0.47 μM, Vmax = 0.66 ± 0.21 pmol·min-1·mg-1; Dol·P Km = 2.08 ± 0.85 μM, Vmax = 0.13 ± 0.06 pmol·min-1·mg-1 protein.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020205
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  • 9
    Electronic Resource
    Electronic Resource
    Storage proteins of the fall webworm, Hyphantria cunea drury (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 115-130 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph ; fat body ; yolk protein ; vitellogenin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two storage proteins, storage protein-1 (SP1) and storage protein-2 (SP2), were found in hemolymph and fat body during the development of Hyphantria cunea, the fall webworm. Both storage proteins show similiar quantitative changes during development in males and females; however, SP1 is more abundant. The hemolymph of last instar larvae contains high concentrations of the storage proteins. However, following pupation, the storage proteins accumulate in fat bodies. SP1 peaks in the hemolymph of males and females late in last instar larvae (8-day-old 7th instar larvae).SP1 has a native molecular weight of 460,000 and consists of six identical subunits (Mr = 76,700), while SP2 has a molecular weight of 450,000 and is composed of two different subunits (Mr = 74,100 and 72,400). Both SP1 and SP2 are hexamers and are phosphorylated glycolipoproteins. The pl values of SP1 and SP2 were determined to be 5.70 and 5.50, respectively.Antibodies raised against SP1 react positively with vitellogenin and ovary extract, as well as with proteins in the hemolymph from last instar larvae and proteins in pupal fat bodies. Storage protein synthesis starts in fat bodies of a 4-day-old 7th instar larvae and in female peaks at 6-8 days of the 7th instar.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100203
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  • 10
    Electronic Resource
    Electronic Resource
    Metabolism of ecdysteroids by a chitin-synthesizing insect cell line (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 15 (1990), S. 137-148 
    Details
    ISSN: 0739-4462
    Keywords: Blatella germanica ; ecdysone ; cholesterol ; tissue culture ; cell culture ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A chitin-synthesizing cockroach cell line (UMBGE-4) previously shown to secrete ecdysteroids was analyzed for its ability to metabolize potential precursors of ecdysone (e.g., 2-deoxyecdysone, 2,22-dideoxyecdysone, 2,22,25-trideoxyecdysone, and cholesterol). All, except cholesterol, were actively metabolized by UMBGE-4 cells. However, all but 2-deoxyecdysone were converted to polar and hydrolyzable metabolites, and not to ecdysone. Labeling with cholesterol was unsuccessful. Labeling experiments with molting hormones, i.e., ecdysone and 20-hydroxyecdysone, confirmed that this cell line can metabolize ecdysteroids and allowed identification of some of the products. Molting hormones were converted into acetate conjugates and polar conjugates which were often double-conjugates, i.e., polar conjugates of acetate conjugates. Labeling experiments with ecdysone demonstrated that this cell line possesses a low ecdysone 20-hydroxylase activity. The capacity of UMBGE-2 cells, which do not synthesize chitin or ecdysteroids, was also examined. Neither ecdysone nor 20-hydroxyecdysone was significantly metabolized by UMBGE-2 cells. 2-Deoxyecdysone and 2,22-dideoxyecdysone were very slowly metabolized respectively to more polar compounds.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940150303
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