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The Nature of a Nematode Growth Factor. I. Growth and Maturation of Caenorhabditis Briggsae On Ribonucleoprotein Particles

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For more content, see Nematology.

The biological activity of ribonucleoprotein (RNP) particles from yeast, E. coli, mammalian liver, HeLa cells and pea seedlings on maturation and reproduction of the free-living nematode Caenorhabditis briggsae has been evaluated. RNP particles from yeast, E. coli, mammalian liver and HeLa cells are biologically highly active. The minimum doses permitting maturation and reproduction within 7 days were 3.4, 13, 9.8, and 3.2 μg protein/ml respectively. The addition of haemin chloride at a final concentration of 10 μg/ml did not improve biological activity. RNP particles from E. coli, washed with 1M salt were inactive. Pea seedling particles were inactive, but became active upon addition of haemin chloride to the medium. It is assumed that the activity of RNP preparations is due to a contaminating haem protein.

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


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