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The Nature of a Nematode Growth Factor. Ii. Growth and Maturation of Caenorhabditis Briggsae On Haem Proteins

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For more content, see Nematology.

The growth promoting activity of cytochrome c, catalase, haemiglobin, myoglobin, horse radish peroxidase, yeast L-lactate dehydrogenase and cytochrome c reductase on maturation and reproduction of Caenorhabditis briggsae has been evaluated. Cytochrome c, catalase, haemiglobin, myoglobin, and horse radish peroxidase were biologically active when properly precipitated. The biological activity of horse radish peroxidase (assayed as the peroxidase-antiperoxidase immunoprecipitate) was greatly increased upon addition of haemin to the medium. This is easily explained on the assumption that much haem could have been split off from the protein during the activation treatment. Yeast L-lactate dehydrogenase and cytochrome c reductase did not contain sufficient amounts of haem after the activation treatment. They were inactive in haemin lacking basal medium, but highly active in basal medium supplemented with haemin. These experiments support the idea that the third and so far unknown component (the other components being sterols and haem) of the growth factor complex is not a protein of particular nature, but rather any convenient vector for the haem component.

Affiliations: 1: Laboratoria voor Morfologie en Systematiek, Museum voor Dierkunde, Rijksuniversiteit Gent, Ledeganckstraat 35, B-9000 Gent (Belgium)


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