Hostname: page-component-cd9895bd7-fscjk Total loading time: 0 Render date: 2024-12-26T00:43:55.764Z Has data issue: false hasContentIssue false
  • English
  • Français

The kinetics of the penetration of some representative anthelmintics and related compounds into Ascaris lumbricoides var. suis

Published online by Cambridge University Press:  06 April 2009

A. R. Trim
A. R. Trim
Affiliation:
Biochemical Laboratory, University of Cambridge
Get access Rights & Permissions [Opens in a new window]

Extract

1. The rate of penetration of some representative drugs into Ascaris lumbricoides var. suis has been measured.

2. The series of 4-n-alkyl resorcinols shows a typical homologous series effect.

3. l-Nicotine penetrates relatively slowly.

4. Its rate of penetration is greatly influenced by the extent of dissociation of its methyl pyrrolidine basic group.

5. The rate of penetration of nicotine is greatly accelerated in the presence of some surface active substances.

6. Chloroform is the most rapidly penetrating substance studied, and its penetration is not significantly influenced by the presence of proteins, carbohydrates and fats and their products of digestion.

7. An analysis of the experimental results shows that the outermost layer of the cuticle of Ascaris is probably the main barrier to penetration. It behaves as if it were a thin; homogeneous layer of lipoid.

8. The significance of these results in the study of anthelmintics is assessed.

Type
Research Article
Information
Parasitology , Volume 39 , Issue 3-4 , February 1949 , pp. 281 - 290
Copyright
Copyright © Cambridge University Press 1949

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Alexander, A. E. & Trim, A. R. (1946). Proc. Roy. Soc. B, 133, 220.Google Scholar
Baldwin, E. (1943). Parasitology, 35, 89.Google Scholar
Berenblum, I. & Chain, E. (1938). Biochem. J. 32, 295.CrossRefGoogle Scholar
Clark, W. M. (1928). The Determination of Hydrogen Ions, pp. 45, 67.Google Scholar
Cole, W. H. (1926). J. Biol. Chem. 71, 173.Google Scholar
Collander, R. (1937). Trans. Faraday Soc. 33, 985.CrossRefGoogle Scholar
Danielli, J. F. (1941). Trans. Faraday Soc. 37 (3), 121.CrossRefGoogle Scholar
Ellisor, L. O. & Richardson, C. H. (1938). J. Cell. Comp. Physiol. 11, 377.CrossRefGoogle Scholar
Ferguson, J. (1939). Proc. Roy. Soc. B, 127, 387.Google Scholar
Hotchkiss, R. D. (1944). Advances in Enzymology, 4, 153.Google Scholar
Jacobs, M. H. (1940). Cold Spr. Harb. Symp. Quant. Biol. 8, 30.Google Scholar
Kolthoff, J. M. (1925). Biochem. Z. 162, 289.Google Scholar
Lamson, P. D., Brown, H. W. & Ward, C. B. (1935). J. Pharm. 53, 198.Google Scholar
Leonard, V. (1924). J. Amer. Med. Ass. 83, 2005.Google Scholar
Parks & Huffman (1932). Free Energies of Some Organic Compounds, Amer. Chem. Soc., Monograph Series, no. 60.Google Scholar
Pigman, W. W. & Richtmyer, N. K. (1942). J. Amer. Chem. Soc. 64, 369.CrossRefGoogle Scholar
Ponder, E. & Hyman, C. (1939). Proc. Soc. Exp. Biol., N.Y., 42, 320.Google Scholar
Trim, A. R. (1944). Parasitology, 35, 209.CrossRefGoogle Scholar
Trim, A. R. (1948). Biochem. J. 43, 57.CrossRefGoogle Scholar