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Translocation of 0,0-diethyl 0, P-nitrophenyl thiophosphate in the American cockroach, Periplaneta americana (L.)Ball, Harold J. January 1951 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1951. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 68-69).
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Muscle succinoxidase in the American cockroach, Periplaneta americana (L.)Harvey, George Thomas, January 1953 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1953. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 70-74).
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On the activity of the spermatozoa of Periplaneta.Hughes, Malcolm. January 1968 (has links)
No description available.
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Light and electron microscope studies of the hemocytes of Periplaneta americana L. (Orthoptera: Blattidae) with special reference to microtubulesBaerwald, Roy James, January 1970 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1970. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
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On the activity of the spermatozoa of Periplaneta.Hughes, Malcolm. January 1968 (has links)
No description available.
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Some aspects of metabolism in Periplaneta americanaWhitehead, D. L. January 1961 (has links)
The structure of insect cuticle has been reviewed briefly and an account given of the processes by which hardening (tanning) occurs after the moult. The sclerotin wall of the cockroach ootheca is formed by the intermingling of the accretions of the left and right colleterial glands. This system, because of its comparative convenience, is studied with a view to shedding light on the sclerotin formation in the cuticle. With reference to their role in sclerotization, the properties of insect blood and cuticle oxidases are reviewed and comparisons made with the animal and plant enzyme grouse they most resemble - tyrosinases and laccases. The function of copper in these oxidases is discussed. A method was developed for determining the protein concentrations, in the presence of phenolic compounds, of the diluted secretion from the left colleterial glands of Periplaneta. This involved digestion (6N-HCl, 6 hours) of the protein followed by estimation with ninhydrin of the total amino acids in the hydrolysate. Investigation of the properties of the copper-containing (0.1-0.2%) phenoloxidase of the left colleterial gland showed that the enzyme is specific towards diphenols (especially ortho-) and is therefore not a tyrosinase. In the majority of its properties the oxidase resembles a laccase, although it is more specific than the plant enzymes. Phenolic substrates bearing an amino group in the side chain are not active - a property which clearly distinguishes the cockroach phenoloxidase from the blood tyrosinase of insects. Towards certain substrates (catechol, hydroquinone, homoprotocatechuic acid) activity is unexpectedly stable to boiling while towards others (protocatechuic acid and its aldehyde) it is destroyed. Possibly non-enzymic, as well as enzymic, activity exists. The effect of some substances (detergents, dopa, catechol, tyrosine, ascorbic acid) on the activity of the phenoloxidase towards protocatechuic acid (3 μmoles) is measured. The stimulation caused by ascorbic acid (0.15 andmu;moles) is related to the possible requirement of cuprous ions for enzyme activity. The phenoloxidase activity which resides in a articulate fraction of the gland secretion, is (unlike other copper oxidases) not inhibited by metal chelating agents, such as phenylthiourea, diethyldithiocarbamate, ethylenediaminetetracetic acid and 4-chlororesorcinol, in the presence of sodium phosphate buffer (0.1M -, pH 6.8). Cyanide and borate are effective inhibitors, however. Varied attempts to purify the participate enzyme and thus to fractionate it from the prosclerotin or structural protein met with little success. The specific activities (Q<sub>O<sub>2</sub></sub>'s) of the supernatants obtained after high speed centrifugation (100,000-182,000 andtimes; g) are approximately five to ten times higher than those (3.93±1.15(10)) of untreated enzyme preparations. An examination of this "purification" led to the conclusion that the enzyme activity appeared to be rather dependent on the state of aggregation of the protein particles. Further evidence of this effect was inferred from the stimulating action of anionic (deoxycholate) and neutral ("Tween") detergents (added prior to buffering) upon phenoloxidase activity. Prior to the institution, as a regular procedure, of dialysis (0.01M-NaCl) of the colleterial gland secretion (to remove endogenous phenolic compounds), a long induction period (ca. 20-60 mins.) before commencement of oxygen uptake by enzyme and substrate was frequently observed. This long period was minimized by the addition of right gland homogenate or ascorbic acid. In section II, the phenolic compounds found in insect cuticle and in cockroach colleterial glands were examined with reference to their biosynthesis and to their role in sclerotization. Protocatechuic acid, its 4-o-β-D-glucoside and p-tyrosine were identified (chromatographically and spectrophotometrically) in homogenates of left colleterial gland. After aerobic incubation (37°C) of these homogenates substances strongly resembling catechol and tyramine were separated by paper chromatography and identified by their u.v. spectral properties after elution. Protocatechuic acid and p-tyrosine, when added (with and without right gland preparation) to homogenates of left glands, increased the production of catechol and tyramine respectively. From densitometric measurements of ferric chloride/ferricyanide sprayed paper chromatograms the aerobic conversion by left gland homogenate of p-tyrosine (1 andmu;mole added) into tyramine (0.62 andmu;moles) was demonstrated, The amine was also separated by absorption on Amberlite-IRC (H<sup>+</sup>). The decarboxylase systems responsible for catechol and tyramine production, whether induced or not, were heat labile. There is some manometric evidence that the former enzyme is located in right gland cells while the latter is present in the larger gland tissue. These findings are made uncertain by the retardation of the reactions in presence of inorganic buffers (and an anaerobic atmosphere) and by extraneous gas evolution particularly during incubation of mixed homogenates of both glands. In the light of some evidence, the possibility that tyramine might be enzymically oxidized by homogenates of left gland is weighed. The significance of such a reaction, together with the decarboxylation of p-tyrosine and protocatechuic acid, is discussed with regard to the biosynthesis of tanning quinones from the p-tyrosine of the insect blood.
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Inulase in the alimentary canals of Periplaneta americana and Blaberus giganteusAdeyinka, Jacob Adeyemi 03 June 2011 (has links)
Inulase had received little attention and there were conflicting statements about its availability in animals.Adapted anthrone-sulfuric acid and Nelson-Somogyi reagents were used for identifying fructose concentration in inulin hydrolyzed by insect and aerobic bacteria extracts as a measure of inulase activity.Bacteria isolated from the insect’s gut were grown in nutrient agar and their extracts were used in hydrolyzing inulin. Aerobic bacteria-free insect extracts were obtained by injecting aureomycin into the gut of the cockroaches.There was no significant aureomycin effect on inulase production by the insects. The greatest inulase activity was around the gastric ceaca region. The major inulase requirement of the insects was met by gastric ceaca region production and not by the bacteria. The assertion that inulase may not be found in animal workd (Bernfeld 1962, Doby 1965, Hoar 1966) is unsupported. Periplaneta americana (Linnaeus) and Blaberus giganteus (Linnaeus) have inulase in their gastric caeca regions.Studies of inulase could lead to better understanding of cockroach physiology and their symbionts. If inulase is eventually synthesized in the laboratory a significant amount of inulin energy would become available to man through the use of synthetic inulase.Honors CollegeBall State UniversityMuncie, IN 47306
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DIFFERENTIAL GENE EXPRESSION IN PERIPLANETA americana IN RESPONSE TO IMMUNIZATION WITH BEE PHOSPHOLIPASE A2Clyne, Erin Michele 11 October 2001 (has links)
No description available.
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DIFFERENTIAL GENE EXPRESSION IN <i>PERIPLANETA AMERICANA</i> IN RESPONSE TO IMMUNIZATION WITH BEE PHOSPHOLIPASE A2Clyne, Erin M. 11 October 2001 (has links)
No description available.
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Population biology and ecology and of Periplaneta americana (L.) in the urban environmentBao, Nonggang 02 October 2007 (has links)
The American cockroach, Periplaneta americana (L.), is an important urban pest due to its ability to invade residential and commercial structures from non-residential reservoirs. Extensive field studies were conducted in a large urban apartment complex, Lincoln Terrace (LT), managed by the Roanoke Redevelopment and Housing Authority (RRHA), in Roanoke, Virginia. Inspection in the RRHA-LT complex corroborated well with other researchers' finding that sewer and storm drainage systems are the principal reservoirs for P. americana population in the temperate urban environn1ent. Investigations provided new evidence that basements of the RRHA-LT apartment buildings served as secondary reservoirs for this pest species. Environmental and ecological parameters that characterize basements as important P. americana population reservoir foci were studied.
Understanding how populations function in the urban environment is as important as identifying P. americana population reservoirs. Over two-years of fleld investigations demonstrated that foraging activity of P. americana was seasonal. A study of a simulated population of caged American cockroaches maintained in a basement environment confirmed that their foraging activity was seasonal. Foraging seasonality characterizes the seasonal pest status of this cockroach species in the temperate urban environment. Therefore, seasonally oriented control or management strategies for this pest species are proposed and discussed.
Lipids, carbohydrates, and proteins of American cockroach adults were analyzed and quantified on a monthly basis for a year. Seasonal foraging activity was reflected by seasonal changes of metabolic reserves in this species. Low foraging activity in the colder, winter months characterized an overwintering period of P. americana populations in the urban environment. Lipids were the principal metabolic reserve for overwintering cockroaches, and accounted for a 22% of dry body weight loss in females and 18% in males. Proteins accounted for approximately 10% of the dry body weight loss for overwintering females and males. Glycogen concentration per unit dry weight increased 11 % to 15% during the overwintering period. This change suggests that glycogen may function as a cold hardiness substance rather than as a energy reserve during overwintering. Nutrient deficits of post-overwintering individuals in the population explained the underlying physiological driving force for significantly ir~creased foraging activities in the spring.
Caged P. americana demonstrated a high reproductive potentia] in the basement environment. High reproductive rate created protein and lipid deficits in adults that required increased foraging for food and increased cannibalism of oothl!cae and young nymphs. Approximately 33% of the oothecae and 28% of nymphs were cannibalized in the caged population. / Ph. D.
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