The Biochemistry of Insect Hemolymph

Wyatt, G.R.

doi:10.1146/annurev.en.06.010161.000451

Cited by 457 publications

(142 citation statements)

References 1 publication

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“…The maximum amylase activity at pH 6.8 observed in the haemolymph in the present study is consistent with the physiological pH of the haemolymph as reported by Wyatt (1961). The optimum pH of 6.8 of haemolymph amylase observed in the present study is in contrast to slightly acidic range reported in a variety of insect species (Baker, 1987;Podoler and Applebaum, 1971;Buonocore et aL, 1976).…”

Section: Discussionsupporting

confidence: 92%

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Abraham

Nagaraju

Datta

1992

Insect Biochemistry and Molecular Biology

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Abstract--Different amylase enzymes were identified by analysis of digestive fluid and haemolymph in diapausing and nondiapausing strains of silkworm, Bombyx mori. The diapausing strain showed negligible digestive amylase activity at a pH range of 3-11, while the nondiapausing strain registered strikingly higher amylase activity at pH 9.2. Higher levels of undigested starch was found in the faecal matter of the diapausing strain, which is consistent with the negligible digestive amylase activity. Developmental specific expression of haemolymph amylase activity was seen in nondiapausing and diapausing strains. In the nondiapausing strain the digestive amylase activity was at its peak during intermoult and depressed during moult. PAGE analysis revealed the occurrence of only anodal digestive and haemolymph amylases in the diapausing strain, whereas both cathodal and anodal enzymes were seen in the digestive fluid and haemolymph of the nondiapausing strain.

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Section: Discussionsupporting

confidence: 92%

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Abraham

Nagaraju

Datta

1992

Insect Biochemistry and Molecular Biology

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“…First, compared with other animals, insects can store fuels at high concentrations in their haemolymph [51]. Carbohydrates are found in high concentration largely owing to the presence of the nonreducing disaccharide trehalose.…”

Section: Discussion (A) Proline Metabolism In Hymenopteransmentioning

confidence: 99%

Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

et al. 2016

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Bees are thought to be strict users of carbohydrates as metabolic fuel for flight. Many insects, however, have the ability to oxidize the amino acid proline at a high rate, which is a unique feature of this group of animals. The presence of proline in the haemolymph of bees and in the nectar of plants led to the hypothesis that plants may produce proline as a metabolic reward for pollinators. We investigated flight muscle metabolism of hymenopteran species using high-resolution respirometry performed on permeabilized muscle fibres. The muscle fibres of the honeybee, Apis mellifera, do not have a detectable capacity to oxidize proline, as those from the migratory locust, Locusta migratoria, used here as an outgroup representative. The closely related bumblebee, Bombus impatiens, can oxidize proline alone and more than doubles its respiratory capacity when proline is combined with carbohydrate-derived substrates. A distant wasp species, Vespula vulgaris, exhibits the same metabolic phenotype as the bumblebee, suggesting that proline oxidation is common in hymenopterans. Using a combination of mitochondrial substrates and inhibitors, we further show that in B. impatiens, proline oxidation provides reducing equivalents and electrons directly to the electron transport system. Together, these findings demonstrate that some bee and wasp species can greatly enhance the oxidation of carbohydrates using proline as fuel for flight.

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“…Inasmuch as the pH of insect hemolymph is known to be slightly acidic [20] we selected 10 mM sodium succinate, pH 5.7, as buffer to examine the effect of ionic strength on the LTP sedimentation velocity pattern. The results revealed an ionic strength-dependent alteration in the sedimentation rate of LTP.…”

Section: Resultsmentioning

confidence: 99%

Biophysical studies on the lipid transfer particle from the hemolymph of the tobacco hornworm, Manduca sexta

Ryan¹,

Hicks²,

Kay³

1990

FEBS Letters

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Hydrodynamic studies conducted in the analytical ultracentrifuge provided evidence for two populations of lipid transfer particle (LTP) when centrifuged in a buffer solution containing 10 mM Tris, pH S.O/lOO mM KCl. The apparent sedimentation coefficients of the two species was 23.3 S and 15.3 S. Upon changing the buffer pH to 7.0 or 5.7, two species of LTP were still present but the ratio of their relative abundance was altered. When the KC1 concentration in the buffer was lowered to 50 mM the sample sedimented as a single species with an apparent s~,~ of 22.9 S. In higher ionic strength buffers (10 mM succinate, pH 5.7/500 mM KCl) LTP sedimented with an apparent s~,~ of 14.8 S. Further experiments revealed that these two forms are interconvertable as a function of buffer ionic strength. Given previous estimates of the molecular size of LTP we concluded that the slower sedimenting peak observed at high ionic strength represents monomeric LTP while the faster sedimenting material observed at low ionic strength is likely to be an aggregated state of LTP. This interpretation is supported by molecular weight determinations made by sedimentation equilibrium experiments conducted in 10 mM succinate, pH 5.7/500 mM KC1 which yielded a particle M,= 887000. Circular dichroism spectra of monomeric LTP sample revealed 6% a-helix, 49% B-sheet, 7% /?-turn and 35% random coil while aggregated LTP contained 13% a-helix, 66% p-sheet and 21% random coil. The transfer activity of the two LTP forms was assayed and found to be the same indicating that either the state of LTP aggregation did not affect transfer activity or that upon exposure to a large excess of lipoprotein substrate disaggregation, without loss of activity, occurs.

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The Biochemistry of Insect Hemolymph

Cited by 457 publications

References 1 publication

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Biochemical studies of amylases in the silkworm, Bombyx mori L.: Comparative analysis in diapausing and nondiapausing strains

Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans

Biophysical studies on the lipid transfer particle from the hemolymph of the tobacco hornworm, Manduca sexta

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