The glyoxylate cycle and the conversion of triglycerides to carbohydrates in developing eggs of Ascaris lumbricoides

Barrett, John; Ward, Colin W.; Fairbairn, Donald

doi:10.1016/0010-406x(70)90974-6

Cited by 83 publications

(28 citation statements)

References 24 publications

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“…It thus appears that the palmitate incorporated into the eggs is highly susceptible to oxidation under air. In other words, since molecular oxygen is an essential requirement for the development of Ascaris eggs (Passey and Fairbairn 1955;Lescure 1965, 1966;Barrett et al 1970), the eggs might utilize certain fatty acids as an energy source during the development under these conditions (Jezyk and Fairbairn 1969).…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of lipids during embryogenesis of Ascaris lumbricoides eggs.

Furukawa

Yamamoto

Kimura

et al. 1985

Tohoku J. Exp. Med.

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Section: Resultsmentioning

confidence: 99%

Biosynthesis of lipids during embryogenesis of Ascaris lumbricoides eggs.

Furukawa

Yamamoto

Kimura

et al. 1985

Tohoku J. Exp. Med.

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“…, and a variety of nematodes (2,10,22). In spite of its central importance in seedling metabolism and development, little is known about catalysis by plant isocitrate lyase.…”

Section: Introductionmentioning

confidence: 99%

“…

ABSTRACT (3), and a variety of nematodes (2,10,22). In spite of its central importance in seedling metabolism and development, little is known about catalysis by plant isocitrate lyase.

The first isolation of isocitrate lyase from plants was described by Khan et al (23).

…”

mentioning

confidence: 99%

“…This cycle is operative in a wide range of microorganisms (30), germinating fatty seeds (3), and a variety of nematodes (2,10,22). In spite of its central importance in seedling metabolism and development, little is known about catalysis by plant isocitrate lyase.…”

mentioning

confidence: 99%

“…' Supported in part by National Science Foundation Grant PCM 7909786. 2 Present address: Roche Institute of Molecular Biology, Nutley, NJ 071 10. 3To whom correspondence should be addressed.…”

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confidence: 99%

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Isocitrate Lyase from Flax

Khan

McFadden²

1982

Plant Physiol.

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(3), and a variety of nematodes (2,10,22). In spite of its central importance in seedling metabolism and development, little is known about catalysis by plant isocitrate lyase.The first isolation of isocitrate lyase from plants was described by Khan et al. (23). Several molecular properties of the enzyme from flax were characterized but data were insufficient to deduce the kinetic mechanism. Moreover, nothing was reported about the structure of the active site. Information about these characteristics of the plant enzyme has remained sketchy. Such information assumes special significance because plant isocitrate lyase functions within cytoplasmic organelles called glyoxysomes (3) whereas the prokaryotic enzyme is operationally 'soluble' (27, 28 (36) with a slight modification. In a total volume of 1.0 ml, the incubation mixture (pH 7.5) contained: 100 ,umol Mops, 5 tmol MgCl2, 2 pmol DTT, 10 ,imol trisodium DL-iSocitrate, and enzyme. After 10 min incubation at 30°C, the reaction was quenched by addition of 0.1 ml of 1 M oxalic acid. A suitable aliquot was diluted to 2.6 ml with distilled H20 followed by the addition of 0.1 ml of 1% (w/v) phenylhydrazine-hydrochloride. After thorough mixing, the tubes were chilled in ice for 10 min, and 1.5 ml prechilled concentrated HCI added with rapid mixing followed after 5 min by addition of 0.1 ml of 5% (w/v) potassium ferricyanide. After thorough mixing and incubation for 15 min at 25°C, the color intensity was read at 520 nm. Reaction rates were proportional to enzyme and the rate was constant over a 25-min incubation period.To examine the inhibition of isocitrate lyase by glyoxylate, the reaction rate was determined by assaying succinate using succinic dehydrogenase (38).The condensation reaction catalyzed by isocitrate lyase was studied as decribed by Johanson et al. (19) by coupling with an excess of NADP+-isocitrate dehydrogenase. Amino Acid Analysis. Isocitrate lyase was exhaustively dialyzed against 0.1 M NaCl prior to amino acid analysis. Aliquots of the dialyzed enzyme were transferred to hydrolysis vials having norleucine as an internal standard and the contents lyophilized. After addition of 0.5 ml of 6 N HCI, the vials were degassed in vacuo and sealed under N2. The hydrolysis was carried out at 1 10°C and all hydrolysates were analyzed with a Beckman 120C automatic amino acid analyzer by the method of Moore and Stein

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Isocitrate lyase activity in the regenerating forelimb of the adult newt

Jasch

Schmidt

1974

J. Exp. Zool.

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Regenerating and non-regenerating limb tissues from the adult newt, Diemictylus viridescens, were assayed for isocitrate lyase activity. The enzyme assays were performed by micromodifications of existing procedures. In general, the whole homogenate, or a soluble fraction of the homogenate, was incubated with the substrate isocitrate. Isocitrate is cleaved by isocitrate lyase to glyoxylate and succinate. At the termination of the reaction, the 2,4-dinitrophenylhydrazone derivative of glyoxylate was produced, extracted and quantitated spectrophotometrically. Isocitrate lyase activity was localized to bulb and two-digit regenerates. The reaction product, glyoxylate (a monocarboxylic keto acid), was of special interest due to its role as a potent in vitro metabolic inhibitor. Therefore, the endogenous level of monocarboxylic keto acids, and the ability of regenerating tissue to produce and accumulate monocarboxylic keto acids, were investigated. Whole homogenates of regenerating tissue always contained more monocarboxylic keto acids than intact forearm or stump tissue.

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The glyoxylate cycle and the conversion of triglycerides to carbohydrates in developing eggs of Ascaris lumbricoides

Cited by 83 publications

References 24 publications

Biosynthesis of lipids during embryogenesis of Ascaris lumbricoides eggs.

Biosynthesis of lipids during embryogenesis of Ascaris lumbricoides eggs.

Isocitrate Lyase from Flax

Isocitrate lyase activity in the regenerating forelimb of the adult newt

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