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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (35)
  • Wiley-Blackwell  (35)
  • Elsevier
  • 1985-1989  (35)
  • 1
    Electronic Resource
    Electronic Resource
    Partial characterization of a major gut thiol proteinase from larvae of Callosobruchus maculatus F. (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 561-575 
    Details
    ISSN: 0739-4462
    Keywords: Callosobruchus maculatus ; proteinase inhibitors ; thiol digestive proteinase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Much of the proteolytic activity in the digestive tract of Callosobruchus maculatus larvae can be attributed to a thiol proteinase(s) that hydrolyzes [3H]methemoglobin optimally at pH 5.0. Maximal hydrolysis of [3H]methemoglobin, [3H]alpha-casein, and N-benzoyl-DL-arginine napthylamide-(BANA) required the presence of thiol reducing agents. Larval gut proteinase activity was strongly inhibited by p-hydroxymercuribenzoic acid (pHMB), Nethylmaleimide (NEM), and iodoacetic acid (IAA) but was unaffected by the Bowman-Birk and Kunitz proteinase inhibitors from soybeans or by lima bean trypsin inhibitor. L-Trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (E-64), a specific inhibitor of thiol proteinases, potently inhibited proteolysis of [3H]methemoglobin by larval gut homogenates. Proteolytic activity in the larval gut was located in the lumen contents and thus appears to play a major role in extracellular digestion. The pH of the larval midgut is slightly acidic, and midgut contents exhibit a negative redox potential, conditions supporting the activity of a thiol proteinase. The significance of these findings is discussed with reference to the vulnerability of this digestive proteinase as a target for existing or genetically engineered plant chemical defenses.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030607
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of conditioned media on three genotypes of Drosophila melanogaster: Physical, chemical, and biological aspects (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 485-497 
    Details
    ISSN: 0739-4462
    Keywords: interactions among genotypes ; uric acid ; biotic residues ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The uric acid contents in larvae, pupae, and culture media were studied during larval and pupal development in three genotypes of Drosophila melanogaster reared in both crowded and noncrowded conditions. The uric acid content and the response of genotypes in media supplemented with 10 and 15 mg/ml of uric acid were correlated with the outcome obtained in conditioned media. In addition, the behavior of genotypes in conditioned media is explained in terms of the physicochemical properties of the conditioned media, which include uric acid content, the amount of food ingested, the degree of free water, the physical disturbance within the cultures, and the particular response of each genotype to uric acid.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030508
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  • 3
    Electronic Resource
    Electronic Resource
    Cuticular lipids for species recognition of mole crickets (Orthoptera: Gryllotalpidae): II. Scapteriscus abbreviatus, S. acletus, S. vicinus, S. sp., and Neocurtilla hexadactyla (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 127-134 
    Details
    ISSN: 0739-4462
    Keywords: Scapteriscus ; cuticular lipids ; hydrocarbons ; gas chromatography ; mole cricket ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Qualitative analyses were made from whole-body cuticular extracts of Scapteriscus abbreviatus, Scapteriscus acletus, Scapteriscus vicinus, and Neocurtilla hexadactyla by isothermal and temperature-programmed gas chromatography. Adults of both sexes and nymphs of each species were collected in Florida. The chromatographic profiles of peaks were distinct and easily recognizable for each species, regardless of sex or developmental stage. Distinct sexual differences were found in S. acletus and S. abbreviatus. Specimens of S. abbreviatus from Puerto Rico and S. vicinus from Bolivia produced gas chromatography (GC) traces very similar to those of conspecifics collected in Florida. Evidence is presented to illustrate the potential importance of volatile cuticular lipid analysis as a tool for mole cricket identification. Cuticular extracts of an undescribed short-winged species of Scapteriscus from Bolivia were also examined and produced GC traces unlike those of any other species analyzed to date.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030203
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  • 4
    Electronic Resource
    Electronic Resource
    Host-plant resistance of sorghum: Differential hydrolysis of sorghum pectic substances by polysaccharases of greenbug biotypes (Schizaphis graminum, homoptera: Aphididae) (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 203-215 
    Details
    ISSN: 0739-4462
    Keywords: greenbug ; Schizaphis ; biotype ; polysaccharases ; probing behavior ; cellulase ; pectinase ; sorghum ; symbiotes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pectic substances extracted from different varieties of sorghum are hydrolyzed at differing rates by unfractionated polysaccharases isolated from two biotypes (C, GBC; and E, GBE) of the sorghum pest, Schizaphis graminum (the greenbug). A higher degree of susceptibility of a sorghum variety is associated with a greater rate of hydrolysis of sorghum pectic substances by a greenbug biotype. Increases in the specific activity of polysaccharases on the pectic substances from a resistant sorghum variety are dependent on the duration that a biotype is maintained as a colony on that variety. Polysaccharase activity of GBE on arabinogalactan was significantly greater than GBC. However, there were no differences between the biotypes on the depolymerization of a variety of other plant matrix polysaccharides and a synthetic polysaccharide. The sequence of substrates of increasing refractoriness to hydrolysis are: arabinogalactan 〈 microcrystalline cellulose 〈 xylan 〈 pectin 〈 2,3-diacetyl pectin 〈 α-1,4-galacturonan. Pectic substances from sorghum varieties resistant to GBC but susceptible to GBE are relatively lower in arabinogalactan with elevated levels of uronic acid (UA) compared to varieties susceptible to both biotypes. A sorghum variety resistant to both GBC and GBE was lowest in levels of arabinogalactan, highest in UA, and highest in fructan content, which in the other varieties occurred only in trace amounts. Pectic composition of rhamnose, xylose, and glucose showed no relationship to resistance. Bound phenolics (potential inhibitors of enzyme activity) were not detected in any of the sorghum pectic substances. The relationship of plant matrix polysaccharides to host-plant aphid biotype compatibility is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020208
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  • 5
    Electronic Resource
    Electronic Resource
    Superoxide dismutase in the housefly, Musca domestica (L.) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 31-43 
    Details
    ISSN: 0739-4462
    Keywords: superoxide dismutase ; housefly ; Musca domestica ; enzyme purification and characterization ; rose bengal ; singlet oxygen ; enzyme deactivation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four superoxide dismutase (SOD) (E.C. 1.15.1.1) isozymes were present in whole tissue homogenates of Musca domestica when examined by polyacrylamide gel electrophoresis. One of the isozymes contained manganese, and the other three contained copper and zinc. All were observed in each of the body tagma (head, abdomen, and thorax) and at each developmental stage (egg to adult).The copper- and zinc-containing isozymes purified from newly emerged, adult M. domestica had a relative molecular weight of 34,800 as determined by gel filtration chromatography but consisted of two equal-size subunits of 16,000 as measured by sodium dodecylsulfate polyacrylamide gel electrophoresis. An isoelectric point between 4.8 and 5.1 was measured. Approximately 2 mol each of copper and zinc were present per dimer. The three copper, zinc isozymes were identified as charge variants. The amino acid composition of the enzyme was similar to that of copper, zinc-containing superoxide dismutases from other sources.Purified housefly copper, zinc superoxide dismutase was neither deactivated nor able to protect lactic dehydrogenase against deactivation in the presence of light and rose bengal, a known generator of singlet oxygen. The role of SOD in the phototoxic reaction involving rose bengal is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030105
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  • 6
    Electronic Resource
    Electronic Resource
    The effect of L-canavanine and L-canaline on the hemolymph amino acid composition of the tobacco hornworm, Manduca sexta (L.) (Sphingidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 265-275 
    Details
    ISSN: 0739-4462
    Keywords: L-canavanine ; L-canaline ; Manduca sexta ; plant-insect interactions ; hemolymph amino acids ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Tobacco hornworm larvae, Manduca sexta (L.) (Sphingidae), were administered L-canaline either by parenteral injection or by dietary consumption. The overt toxicity and the alteration of hemolymph amino acids caused by these nonprotein amino acids were evaluated. The LD50 value for parenterally administered canavanine and canaline is 1.0 and 2.5 mg/g fresh body weight, respectively. A dietary concentration of 5.2 mM for canavanine and over 20 mM for canaline represent the respective LC50 values. A large percentage of the larvae reared on diets supplemented with additional arginine, ornithine, or 2,4-diaminobutyric acid in addition to canavanine or canaline were unable to complete larval-pupal ecdysis. These toxic effects were associated with a decreased glutamic acid hemolymph titer and dramatically elevated ornithine. On the other hand, larvae administered canavanine or canaline alone, either by dietary consumption or parenteral injection, experienced less drastic developmental aberrations. These symptoms were in some cases correlated with increased ornithine and glutamic acid titers. Evidence is presented that even a canavanine- and canaline-sensitive insect such as M. sexta has a marked ability to eliminate these protective allelochemicals.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030305
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  • 7
    Electronic Resource
    Electronic Resource
    Posteclosion behavior of the flesh fly, Sarcophaga crassipalpis: A comparison of wild-type and unicorn mutants (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 101-106 
    Details
    ISSN: 0739-4462
    Keywords: eclosion behavior ; emergence ; hemolymph pressure ; pulsing ; pumping ; grooming ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Newly emerged flies go through a stereotypic behavioral pattern of walking, grooming, abdomen contraction (pulsing), and active uptake of air (pumping). These behavioral activities can be readily distinguished on the basis of hemolymph pressure changes. Wild-type flies and a unicorn mutant that fails to properly retract its ptilinum show identical patterns of posteclosion activity. However, a portion of the unicorns do not fully expand their wings and abdomen. Such flies are missing only the pumping component of the normal behavioral repertory, thus implying that pulsing and pumping are independently controlled.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940040203
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis of proteins and nucleic acids by the pea aphid Acyrthosiphon pisum (aphididae) in the absence of a full complement of dietary amino acids (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 161-168 
    Details
    ISSN: 0739-4462
    Keywords: aphids ; nucleotides ; sucrose ; symbionts ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Protein, nucleic acids, and nucleotide syntheses were studied in pea aphids, Acyrthosiphon pisum (Harris), by feeding them labeled 14C-amino acids and [5-3H]-orotic acid in sucrose. It was demonstrated that in the absence of dietary essential amino acids, aphids were capable of synthesizing nucleic acids, nucleotides, and proteins when provided with a single dietary amino acid in sucrose. It is suggested that other required amino acids were possibly supplied by the symbionts present in the pea aphid and/or were obtained from the amino acid pool in the hemolymph or glucose, one of the end products of sucrose digestion. Of the various amino acids tested, synthesis of measurable amounts of protein or other compounds occurred when alanine, aspartic acid, glutamic acid, glycine, proline, or serine were provided, but no synthesis occurred with cysteine.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940040302
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  • 9
    Electronic Resource
    Electronic Resource
    Novel assay for determining the metabolic fate of juvenile hormone III: A study with Drosophila melanogaster (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 25-37 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone ; epoxide hydrolase ; JH esterase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A thin-layer chromatographic assay was developed for the resolution of hydrolytic and conjugative catabolites of juvenile hormone (JH). A single-dimension, dual-development thin-layer system allowed complete resolution of the catabolites. Thus, this system provided a means for the rapid and economic analysis of JH hydrolysis even when different hydrolytic activities were present concurrently. Purified hydrolytic enzymes were found to be superior to chemical methods for the generation of small amounts of standards of JH catabolites. The relative levels of activities of an epoxide hydrolase and an esterase toward JH III were found to be similar in microsomal preparations from three lines of adult Drosophila melanogaster isolated from a field population. However, selection of flies by exposure to cut orange resulted in the elevation of levels of epoxide hydrolase activities, whereas esterase levels were not affected to the same extent. The formation of the JH acid-diol was not detected under the conditions of this study, suggesting that the JH acid and diol were not good substrates for epoxide hydrolase and juvenile hormone esterase, respectively.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080104
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  • 10
    Electronic Resource
    Electronic Resource
    Degradation of aberrant proteins by larval tobacco hornworm, Manduca sexta L. (Sphingidae) (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 165-172 
    Details
    ISSN: 0739-4462
    Keywords: L-canavanine ; plant-insect interactions ; canavanyl protein ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The tobacco hornworm Manduca sexta (Sphingidae) readily incorporates L-canavanine, the L-2-amino-4-(guanidinooxy)butyric acid structural analog of L-arginine, into newly synthesized proteins. As a result, the developing fifth-instar larva produces structurally aberrant canavanyl proteins that can exhibit severely impaired function. This situation is exacerbated by canavanine's ability to stimulate de novo protein synthesis. M. sexta larvae can respond to anomalous protein production by degrading canavanyl proteins nearly five times faster than normal proteins. The proteases of this insect can distinguish between normal and anomalous proteins and thereby avoid destruction of essential macromolecules. Aberrant protein degradative activity is not dependent upon de novo protein synthesis induced by canavanyl proteins. The fat body appears to be the source of proteases that degrade aberrant proteins; degradation is curtailed in the presence of sulfhydryl protease inhibitors as well as inhibitors of trypsin-like activity.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080303
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