242
PHOSPHATASES IN EIMERIA TENELLA
[ Vol. XXIV, Part IV,
and Brachet [1947]. Possibly protein synthesis involves the formation of a phos-
phoprotein and that the action of phosphatases in nuclei is to split off the phosphate
residue from protein, and thus liberating an active product from an inactive precursor
[Danielli, 1953].
In support of the conclusions drawn, with regard to the relation of RNA to
alkaline phosphatan in protein metabolism of E. tenella, many parallel references to
similar studies on mammalian tissues can be cited. But, since this is not within
the scope of this article, the reader is referred to the works of Brachet, Danielli,
Caspersson and their colleagues.
Relation between phosphatases and mucopolysaccharides of E. tenella
The cytoplasmic distribution of alkaline and acid phosphatase in the second
generation merozoites is of considerable interest. The site of location of these
enzymes is an area 2-3 µ long, situated immediately anterior to the nucleus. This
area of the organism stains intra-vitam with neutral red. By osmication this very
region turns black. Both these techniques visualise ' Golgi ' elements in cells.
Sulphated acid polysaccharides (metachromatic), 1, 2 glycol groups (Hotchkiss
positive), hyaluronic acid type polysaccharide (Hale positive) alkaline phosphatase
and sometimes acid phosphatase too are present all together in the ' Golgi ' region
of the merozoite. Their simultaneous occurrence naturally suggests a functional
relationship between them. Localisation of alkaline phosphatase activity in the
' Golgi ' region of several metazoon cells has been reported by several workers
[Bourne, 1943 ; Wislocki and Dempsey, 1946 ; Emmel, 1945 : 1946 ; 1947 ; Al
Hussaini, 1948]. Precise functional relationship between the ' Golgi ' element and
alkaline phosphatase has not been understood. Emmel [1946], however, suggests
that the ' Golgi' apparatus synthesizes and secretes alkaline phosphatase. The
latter may well be concerned with the processes of dephosphorylation and deposition
of glycogen [Wislocki and Dempsey, 1946]. In a previous article in the series
glycogen has been shown to be present in the parasite in fair amounts.
Hyaluronic acid type polysaccharide is invariably present in the karyosome
of the parasite and so is the alkaline phosphatase. Further, there is a small pro-
portion of merozoites which do not show any reaction in the 'Golgi' region either for
this enzyme or for hyaluronic acid type polysaccharide. This finding suggests
a still closer metabolic association between alkaline phosphatase and this polysac-
charide. The other acid polysaccharide (i.e. the sulphated one) is only confined to,
and is always present in the ' Golgi ' region. The peripheral globules of macro-
gametes show intense alkaline phosphatase activity. These structures have been
shown to contain RNA and hyaluronic acid type polysaccharide (Refer to previous
communication in the series). At fertilisation these globules coalesce to form oocystic
wall. The latter reacts strongly for hyaluronic acid and RNA and also gives a
moderately positive reaction for alkaline phosphatase. This further supports the
observation that the phosphatase is somehow concerned with the metabolism of acid
polysaccharides and nucleoproteins. Occurrence of alkaline phosphatase and acid
polysaccharides at some sites of a cell, is of particular interest since Sylvén [1947]
reported that in endochondral ossification, chondroitin sulphate disappears in the
cartilage matrix as alkaline phosphatase increases. This observation on E. tenella