Nematode biochemistry

Rothstein, Morton; Mayoh, Helen

doi:10.1016/0003-9861(64)90364-9

Cited by 42 publications

(2 citation statements)

References 23 publications

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“…The ability of free-living nematodes to utilise two-carbon compounds (e.g. acetic acid and ethanol) as an energy source in axenic medium was first demonstrated in three rhabditid species: C. briggsae , T. aceti and P. redivivus [141–143]. Supplementation of ethanol, n-propanol and potassium acetate has stimulatory effects on population growth of C. briggsae in CbMM [51].…”

Section: Caloric Compounds and Building Blocksmentioning

confidence: 99%

The nutritional requirements of Caenorhabditis elegans

2019

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Animals require sufficient intake of a variety of nutrients to support their development, somatic maintenance and reproduction. An adequate diet provides cell building blocks, chemical energy to drive cellular processes and essential nutrients that cannot be synthesised by the animal, or at least not in the required amounts. Dietary requirements of nematodes, including Caenorhabditis elegans have been extensively studied with the major aim to develop a chemically defined axenic medium that would support their growth and reproduction. At the same time, these studies helped elucidating important aspects of nutrition-related biochemistry and metabolism as well as the establishment of C. elegans as a powerful model in studying evolutionarily conserved pathways, and the influence of the diet on health.

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Section: Caloric Compounds and Building Blocksmentioning

confidence: 99%

The nutritional requirements of Caenorhabditis elegans

2019

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“…The cycle is found in bacteria, algae, protozoa, fungi, and plants, but has not been found in mammals. In fact, the first unequivocal report of isocitrate lyase in a multicellular animal was made by Rothstein and Mayoh (1964), who found the enzyme in the free-living nematode, Caenorhabditis briggsae. Subsequently, the enzyme was found in other free-living nematodes (Rothstein and Mayoh, 1965) as well as the companion enzyme of the glyoxylate cycle, malate synthetase (Rothstein and Mayoh, 1966).…”

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confidence: 99%

Isocitrate lyase from the free-living nematode, Turbatrix aceti. Purification and properties

Reiss¹,

Rothstein²

1974

Biochemistry

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Isocitrate lyase (D,-iSOCitrate glyoxylate-lyase, EC 4.1.3.1) has been purified from the free-living nematode Turbatrix aceti. The purified enzyme preparation consists of five isozymes which separate clearly on polyacrylamide gels. A method for the direct assay of activity on the gel is described. Molecular weight determination by gel filtration on Bio-Gel A-15m gave a value of 480,000 for the isozyme mixture. Electrophoresis in the presence of sodium dodecyl sulfate resulted in the appearance of a single sharp protein band having a molecular weight of 123,000. Thus, the enzyme appears to consist of four subunits. The isozyme mixture re-

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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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Nematode biochemistry

Cited by 42 publications

References 23 publications

The nutritional requirements of Caenorhabditis elegans

The nutritional requirements of Caenorhabditis elegans

Isocitrate lyase from the free-living nematode, Turbatrix aceti. Purification and properties

Isocitrate lyase activity in the regenerating forelimb of the adult newt

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