December, 1954]
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is similar to that of Montagna and others [1952] who also found the two substances,
(i.e. the phosphatase and acid polysaccharides) occurring simultaneously in the
papillæ of growing hair follicles (the two analogies are, however, drawn from two
different places, i.e. from protozoa and metazoa respectively).
Alkaline phosphatase activity is depressed in the parasitised regions of caecal
tissue. This differential change in the distribution of the enzyme in healthy and
parasitised tissue is affected to an appreciable degree only when the parasite is
undergoing second generation schizogony. However, no such differential reaction
between healthy and parasitised mucosa could be observed for acid phos-
phatase. This observation is in contrast to that of Carrera [1950], who observed
that there occurred intense acid phosphatase activity in and around amoebic (En-
tamoeba histolytica) ulcers in caeca of experimentally infected guinea-pigs.
The inner and adventitious coats of blood vessels and coarse granules of ' mast '
cells reacted strongly for alkaline phosphatase. ' Mast ' cells are known to originate
from tunica adventitia of small blood vessels [Riley, 1953] and their granules have
been shown to be strongly metachromatic as they contain heparin [Holmgren and
Wilander, 1937]. Thus it seems quite possible that alkaline phosphatase participates
in the elaboration of heparin, and similar other polysaccharide sulphates. Such a
suggestion has already been made by Riley and Drennan [1949] in their studies on
' mast ' cells of rats.
5-Nucleotidase being a specific phosphatase liberates phosphate from 5-nucleoti-
dase. It is distributed in tissues of man and other animals, especially in the poison
gland of snakes. It plays similar, but specific role in nucleoprotein metabolism
as the alkaline and acid phosphomonoesterases. Various combinations of snake
venom phosphatase dephosphorylate RNA to an extent of 75 per cent. [Gulland
and Jackson, 1938], though gut phosphatase is even the more active in this respect,
and completely dephosphorylates this substance [Schmidt and Tannhausser, 1943].
This enzyme has occurred throughout in the nuclei of E. tenella along with alkaline
and acid phosphatase. Occurrence of alkaline phosphatase and 5-nucleotidase
together in the same structure is of interest as they are known not to occur simul-
taneously in certain mammalian tissues investigated so far. Presence of 5-nu-
cleotidase and the absence of alkaline phosphatase is known in renal glomeruli of
obsolescent human beings [McManus, et al., 1952] and in epithelium and secretion
of rattle snake venom glands [Bragdon and McManus, 1953].
SUMMARY
Distribution of acid phosphatase and 5-nucleotidase has been described from
E. tenella. Probable roles played by these two enzymes and alkaline phosphatase
(communicated earlier) in protein and polysaccharide metabolism of the parasite
have been discussed at length.
ACKNOWLEDGEMENT
The authors are indebted to the Indian Council of Agricultural Research, New
Delhi, for the award of Research Fellowship in Parasitology (1952-54) to one of them
(B.S.G.) ; and also to the Director, Indian Veterinary Research Institute, Izatnagar
for providing the necessary laboratory facilities.
104 AR/54.
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