In vitro uptake of C14-labeled alanine and glucose by Ascaridia galli (nematoda) of chickens

Weatherly, Norman F.; Hansen, M. F.; Moser, H. C.

doi:10.1016/0014-4894(63)90007-9

Cited by 17 publications

(3 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results of studies on hexose phosphorylation suggested that A. galli contained non-specific hexokinases equally effective on glucose, mannose and galactose. This observation is in accordance with the earlier findings of Weatherly et al (1963) on the ability of the worms to assimilate labelled glucose by cuticular absorption. The role of hexokinase in the interconversion of the hexoses and channelling the products into the glycolytic pathway would be dependent on the accessory enzymes particularly the UDPG mediated enzymes.…”

Section: Biochemistry Of Ascaridia Galli 169 Discussionsupporting

confidence: 93%

Ascaridia galli: lactic acid production, glycogen content, glycolytic enzymes and properties of purified aldolase, enolase and glucose-6-phosphate dehydrogenase

1970

View full text Add to dashboard Cite

SUMMARYGlycogen reserves of whole worms and their body wall, intestines, ovarian and testicular tubules of the avian intestinal nematode, Ascaridia galli, were assayed and on dry-weight basis found to be 14–20 %, except in the testicular tissue which contained only 7 % glycogen.Segments of whole male worms or testicular tubules were found to produce more lactic acid than segments of whole female worms or ovarian tubules. The body wall and intestine of the worms had also appreciable glycolytic activity. Whereas in the segments of whole worms, male and female alike, glycolysis was more active under anaerobic conditions, no differences in glycolytic rates were seen between aerobiosis and anaerobiosis when isolated tissues were used. Exogenously added glucose did not stimulate glycolysis either aerobically or anaerobically to any extent greater than observed in the absence of glucose.Homogenates of whole worms or their different anatomical parts were assayed for enzymic activities associated with the Embden-Meyerhof pathway of glucose assimilation. The crude extracts prior to differential centrifugation, were found to contain glycogen phosphorylase, aldokinases, pyruvate kinase, phosphatases acting on glucose 6-phosphate and hexose diphosphate and 6-phospho-gluconate dehydrogenase. The 105000 g particulate-free supernate was found to have significant activities of the following enzymes: fructokinase, phosphoglucomutase, phosphoglucoseisomerase, phosphofructokinase, aldolase, glyceraldehyde 3-phosphate dehydrogenase, lactic dehydrogenase and glucose-6-phosphate dehydrogenase. This fraction was devoid of NADH or NADPH oxidase activities in the absence of added substrates.Although there was some indication of a negative correlation between low glycogen reserves and high glycolytic activity in the testicular tubules, in general, there was no relationship between glycogen reserve and glycolytic activity on the one hand or between the rate of glycolysis and the specific activities of some of the key glycolytic enzymes in either whole worm or in tissues other than the testicular tubules.The 105000 g supernate was fractionated with ammonium sulphate. The fraction precipitating between 25 and 80 % saturation of the salt was recovered, dialysed and chromatographed on DEAE cellulose column. By a step-wise elution schedule using increasing molarity of NaCl in tris-HCl buffer, pH 7·4, three main protein fractions were obtained representing respectively enolase, aldolase and glucose-6-phosphate dehydrogenase.The recovery of enzyme activity after chromatography on DEAE cellulose was higher than the amount applied to the column suggesting that during the fractionation some naturally occurring inhibitors were removed. About 10- to 20-fold purification of the enzymes was achieved by anion-exchange chromatography.Some properties of the purified enzymes were studied with respect to the affects of enzyme and substrate concentrations, temperature of preincubation and action of divalent cations, some anions, metal chelating agents and SH reagents. The Km values of enolase, aldolase and glucose-6-phosphate dehydrogenase of A. galli were 5·9 × 10−4M, 4·5 × 10−3M and 2·4 × 10−3M respectively. Glucose-6-phosphate dehydrogenase was found to be very sensitive to both heat and cold losing activity rapidly even at 43 °C or by freezing and thawing.The SH groups of aldolase were readily blocked by pCMB and presumably by o–phenanthroline. No requirement of any divalent cations was shown by this enzyme which was, however, inhibited by borate ions.Enolase of A. galli showed a requirement of Mg2+ for full activation. Phosphate, fluoride, EDTA, o–phenanthroline, αα-bipyridyl inhibited the enzyme. Veronal was found to inactivate the enzyme.Glucose-6-phosphate dehydrogenase of A. galli was also found to be sensitive to SH reagents and metal chelating agents. The enzyme was activated by Co2+, Mn2+ and Mg2+.The evidence presented indicates that segments of whole worms of A. galli or its anatomical parts are equipped with the enzymatic machinery required to mediate anaerobic breakdown of glucose and to derive energy by this mechanism.The authors are grateful to Dr R. K. Kaushik for help in identifying the worms, to Mr P. A. George for help in the statistical analysis of the data and to Messrs A. C. Kol and S. K. Bose for skilful technical assistance.

show abstract

Section: Biochemistry Of Ascaridia Galli 169 Discussionsupporting

confidence: 93%

Ascaridia galli: lactic acid production, glycogen content, glycolytic enzymes and properties of purified aldolase, enolase and glucose-6-phosphate dehydrogenase

1970

View full text Add to dashboard Cite

show abstract

“…Subsequently, many authors have attempted to define the role of the nematode's cuticle as an absorptive surface. Alanine and glucose enter Ascaridia galli through both the intestine and cuticle (Weatherly, Hansen & Moser, 1963), but calculations of the relative roles of these surfaces lead Roberts & Fairbairn (1965) to state that 'the hypothesis of cuticular S i l l "feeding" in nematode parasites should be abandoned'. Castro & Fairbairn (1969a) reached a similar conclusion when they calculated that less than 2 % of the total glucose absorbed by A. suum enters via the cuticle.…”

Section: Physiological Factors Important In Determining the Relative mentioning

confidence: 99%

The relative roles of the intestines and external surfaces in the nutrition of monogeneans, digeneans and nematodes

Pappas

1988

Parasitology

View full text Add to dashboard Cite

Several major groups of parasitic helminths (Monogenea, Digenea and Nematoda) possess two surfaces that are potentially absorptive in nature. These are an external surface, a tegument in the platyhelminths and cuticle in the nematodes, and the intestine. This paper discusses the relative contributions of these absorptive surfaces in the nutrition of these parasitic helminths. There are many factors that determine the availability of, and a parasite's ability to absorb nutrients via either of these surfaces, and this review discusses individually some of the more important morphological, physiological and environmental factors affecting the potential nutritional roles of these surfaces. It is clear from such a summary of previous studies that the intestines and teguments (cuticles) of helminth parasites can each serve an important nutritional role. However, insufficient data make it impossible at this time to determine the relative nutritional roles of these surfaces in any single parasitic helminth.

show abstract

“…After one hour the worms were removed from the medium and washed several times with BFM to remove the adhering radioactivity, transferred to scintillation vials and dissolved in hyminehydroxide solution. The filariids were ligated by collodion treatment (WEATHERLY et al, 1963), both ends being first dipped in acetone and then coated with collodion by two successive dippings.…”

Section: Uptake Studiesmentioning

confidence: 99%

Uptake of adenosine 3′, 5′-cyclic monophosphate and isoproterenol by filarial parasites

et al. 1983

View full text Add to dashboard Cite

The filarial parasites Litomosoides carinii and Dipetalonema viteae both show transcuticular uptake of adenosine 3′, 5′-cyclic monophosphate but isoproterenol is taken up by D. viteae only. The importance of this difference is discussed from the point of view of metabolic regulation. Inhibition of uptake by lectins indicates the involvement of surface sugar moieties in the transport processes.

show abstract

In vitro uptake of C14-labeled alanine and glucose by Ascaridia galli (nematoda) of chickens

Cited by 17 publications

References 21 publications

Ascaridia galli: lactic acid production, glycogen content, glycolytic enzymes and properties of purified aldolase, enolase and glucose-6-phosphate dehydrogenase

Ascaridia galli: lactic acid production, glycogen content, glycolytic enzymes and properties of purified aldolase, enolase and glucose-6-phosphate dehydrogenase

The relative roles of the intestines and external surfaces in the nutrition of monogeneans, digeneans and nematodes

Uptake of adenosine 3′, 5′-cyclic monophosphate and isoproterenol by filarial parasites

Contact Info

Product

Resources

About