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Influence of Enzymes on Germination of Sporocysts Of the Gregarine Pyxinia crystalligera Frenzel *
Author(s) -
KOZLOFF EUGENE N.,
BROWN HAROLD E.
Publication year - 1963
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1963.tb01691.x
Subject(s) - trypsin , germination , lipase , enzyme , sodium , chemistry , biochemistry , chromatography , food science , biology , botany , organic chemistry
SYNOPSIS. Sporocysts of P. crystalligera readily germinate to permit escape of their sporozoites when placed in an infusion of the contents and the tissue of the midgut of the beetle host, Dermestes vulpinus. To determine the type of digestive enzyme required for germination to take place, sporocysts were exposed in hanging drops to 0.25% (w/v) concentrations of commercial preparations of trypsin and lipase in a saline solution. Sodium taurocholate was used in combination with certain of the enzyme preparations. Up to 99% of the sporocysts exposed to trypsin 1:300 and to a relatively crude preparation of lipase (containing some trypsin) germinated within three hours. A refined preparation of trypsin (2 × crystallized, salt‐free) induced up to 65% of the sporocysts to germinate within three hours. Refined lipase (50μl CO 2 /mg/30 min.) had no germinating effect upon sporocysts, either by itself or in combination with sodium taurocholate. In mixtures, crystallized trypsin seemed definitely to be inhibited by sodium taurocholate, and perhaps was inhibited also by refined lipase. The fact that trypsin is effective in causing germination to take place suggests that the germination of sporocysts in the digestive tract of D. vulpinus depends upon a proteolytic enzyme. Unlike trypsin, which was more active in solutions adjusted to an initial pH of 7.0 and 8.0 (especially the latter, in the case of crystallized trypsin) than in those of pH 6.0, this enzyme was more effective in inducing germination at pH values of 6.0 and 7.0.