Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-24T12:12:41.254Z Has data issue: false hasContentIssue false
  • English
  • Français

Digestion in Leidynema appendiculata (Leidy, 1850), a nematode parasitic in cockroaches

Published online by Cambridge University Press:  06 April 2009

D. L. Lee
D. L. Lee
Affiliation:
The Molteno Institute, University of Cambridge
Get access Rights & Permissions [Opens in a new window]

Extract

1. A study of the digestive enzymes present in the nematode Leidynema appendiculata, parasitic in the cockroach, gave the following results.

2. An amylase with optimum activity at pH 4·5, is present. Sodium chloride increases activity by 29 % at this pH.

3. A maltase, with maximum activity at pH 5·0–6·0, is present. It is completely inhibited by 15 % glycerin.

4. Lactase and invertase were not detected.

5. A protease, capable of clotting calcified milk, and of splitting gelatin and edestin, with maximum activity at pH 6·0, is present. KCN does not increase activity.

6. Peptidases splitting glycyl-glycine, dl-leucyl-glycine and dl-leucyl-glycyl-glycine, and a prolidase splitting glycyl-l-proline are present.

7. A lipase hydrolysing glycerol tributyrate, with maximum activity at pH 7·0 is present. Hydrolysis of olive oil and ethyl butyrate was not detected.

8. It is concluded that these enzymes are quite distinct from those of the host and that digestion probably takes place over the range of pH 5·5–6·0.

Type
Research Article
Information
Parasitology , Volume 48 , Issue 3-4 , November 1958 , pp. 437 - 447
Copyright
Copyright © Cambridge University Press 1958

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

Blacklock, D. B., Gordon, R. M. & Fine, J. (1930). Metazoan immunity: A report on recent investigations. Ann. Trop. Med. Parasit. 24, 5–54.CrossRefGoogle Scholar
Carpenter, M. F. P. (1952). The digestive enzymes of Ascaris lumbricoides var. suis; their properties and distribution in the alimentary canal. Dissertation, Univ. Michigan. Univ. Microfilms, Publ. no. 3729. Ann Arbor, Mich. 183 pp.Google Scholar
Chitwood, B. G. (1932). A synopsis of the nematodes parasitic in insects of the family Blattidae. Z. Parasitenk. 5, 14–50.CrossRefGoogle Scholar
Cole, S. W. (1955). Practical Physiological Chemistry, 10th ed. Revised by Baldwin, E. & Bell, D. J.Cambridge: Heffer.Google Scholar
Evans, W. A. L. (1956). Studies on the digestive enzymes of the blowfly Calliphora erythrocephala. I. The carbohydrases. Exp. Parasitol. 5, 191–206.CrossRefGoogle ScholarPubMed
Fodor, P. J. (1948). The specific inhibition by sodium taurocholate of part of the lipolytic enzyme systems contained in extracts from various organs of the grasshopper (Schistocerca gregaria Forsk. and Dociostaurus moroccanus Thnb.). Enzymologia, 12, 333–42.Google Scholar
Hagedorn, H. C. & Jensen, B. N. (1923). Zur Mikrobestimmung des Blutzuckers mittels Ferricyanid. Biochem. Z. 135, 46–58.Google Scholar
Rogers, W. P. (1940). Digestion in parasitic nematodes. I. The digestion of carbohydrates. J. Helminth. 18, 143–54.CrossRefGoogle Scholar
Rogers, W. P. (1941 a). Digestion in parasitic nematodes. II. The digestion of fats. J. Helminth. 19, 35–46.CrossRefGoogle Scholar
Rogers, W. P. (1941 b). Digestion in parasitic nematodes. III. The digestion of proteins. J. Helminth. 19, 47–58.CrossRefGoogle Scholar
Wigglesworth, V. B. (1927 a). Digestion in the cockroach. I. The hydrogen-ion concentration. Biochem. J. 21, 791–6.CrossRefGoogle ScholarPubMed
Wigglesworth, V. B. (1927 b). Digestion in the cockroach. II. The digestion of carbohydrates. Biochem. J. 21, 797–811.CrossRefGoogle Scholar
Wigglesworth, V. B. (1928). Digestion in the cockroach. III. The digestion of proteins and fats. Biochem. J. 22, 150–61.CrossRefGoogle Scholar