The Chemical nature and mode of stabilization of the eggshell/capsule of Moniezia expansa, Avitellinalahorea and Stilesia globipunctata have been investigated using histochemical techniques. In M. expansa Where vitelline glands are present, the eggshell is stabilized by -S-S and -S-H linkages Whereas in A. lahorea and S. globipunctata, the viteline glands are absent and the double membranes, fibrous capsule and paruterine organ contain mainly elastokeratin-type structural protein. The possible role of the vitellaria in the presence or absence of eggshell and its thickness is discussed.

The protein content of fresh homogenates and their corresponding TCA precipitated fractions of 10 different species of helminths was estimated by the methods of Lowry et al. and Spector using the Folin phenol reagent and Coomassie brilliant blue G-250 respectively. The former method gives exaggerated values as compared to the latter method. The parasite phenols, phenolic proteins and catecholamines could be responsible for interference in the Lowry's procedure. The TCA non-precipitable moieties also give colour only with the Folin phenol assay. The pronounced intra-specific differences in the total protein content of helminths reflect their metabolic variations and adaptations. Habitat does not appear to influence the protein content of parasites, however, the effect of host variation was evident in the pouched amphistome G. crumenifer. It is concluded that the dye binding method gives more consistent results and it can be conveniently applied to crude tissue homogenates of helminths.

Mebendazole (3.3 μmol), causes in vitro glycogen depletion and inhibits glucose uptake in Avitellina lahorea. Inhibition of non-specific phosphomonoesterases and adenosine triphosphatase by mebendazole is discussed in the light of the role of phosphatases in uptake mechanisms. Mebendazole has no effect on hexokinase which has broad substrate specificity but influences the activities of some glycolytic enzymes such as phosphorylase, phosphoglucomutase and glucose-6-phosphatase. Thus, it appears that mebendazole also acts to disrupt certain enzymes of carbohydrate metabolism which may ultimately cause death of the parasite.