Abstract
SUMMARY1. It has been shown that the protein eggshell ofHymenolepis diminutaeggs was not significantly stabilized by sulphur or electrovalent linkages but was resistant to attack by proteolytic enzymes. Amino acid analysis demonstrated a marked preponderance of aromatic and heterocyclic acids and it has been suggested that these groups act as cross-linking agents in the shell protein.2. The role of the lipid-containing subshell ‘membrane’ in protecting the enclosed embryo against fluctuations in pH and osmolarity in the external environment and infiltration of enzymes and toxic compounds has been demonstrated.3. The cytoplasmic layer was shown to consist of a glucosamine-containing mucoprotein present in a dehydrated or semi-dehydrated state in the intact egg.In mechanically damaged eggs the cytoplasmic layer was rapidly dispersed by some proteolytic enzymes.4. The embryophore enclosing the hexacanth embryo was composed of a sulphurrich protein that was weakened by some proteolytic enzymes and completely destroyed by others.I should like to thank Professor T. R. E. Southwood, in whose department this work was carried out, and Dr June Mahon for her advice and encouragement.I am particularly grateful to Dr R. A. Wilson, Department of Biology, University of York, for the quantitative amino acid determinations on eggshell hydrolysates and for criticizing this manuscript. This research was conducted during the tenure of a Science Research Council Studentship and formed part of a thesis submitted for the Ph.D. degree, University of London.
Publisher
Cambridge University Press (CUP)
Subject
Infectious Diseases,Animal Science and Zoology,Parasitology
Cited by
18 articles.
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