Protease activity in female Ornithodoros tholozani ticks.
The protease activity in guts of Ornithodoros tholozani females was studied in vitro. The intracellular protease in Ornithodoros tholozani guts has a pH optimum of about 3.0. Hemoglobin is the preferred substrate, and bovine serum albumin is digested very slowly. In this respect the protease resembles cathepsin D. Unfed ticks contain a small amount of protease in the gut. After feeding the level of protease increases gradually for several days until peak protease activity is attained. The level of gut protease activity depends on the size of the blood meal taken and on the interval after feeding. After a period of peak protease activity, the level of protease declines. The level of gut protease in unmated females (kept at 27 degrees C) did not reach prefeeding levels within 100 days. The level of gut proteolytic activity, as determined by in vitro protease assays, does not reflect the degree of blood digestion which takes place in vivo. After a period of rapid digestion, lasting for about two weeks, the undigested part of the blood meal remains unchanged in the lumen of the gut. At that time the gut tissue contains considerable levels of protease, which can be demonstrated by in vitro assays. Presumably, the protease remains active inside the gut cells, although the uptake of hemoglobin from the gut lumen has ceased. The results are compared to those obtained in other tick species.
D000818:Animals; D001769:Blood; D005247:Feeding Behavior; D005260:Female; D006454:Hemoglobins; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000378:metabolism*; D012710:Serum Albumin, Bovine; D013987:Ticks / Q000201:enzymology*
D006454:Hemoglobins; D012710:Serum Albumin, Bovine; D010447:Peptide Hydrolases