2002
DOI: 10.1007/s00436-002-0597-4
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Biochemical comparison of the serine protease (elastase) activities in cercarial secretions from Trichobilharzia ocellata and Schistosoma mansoni

Abstract: We report on serine protease activity in cercarial secretions (CSs) from the bird parasite Trichobilharzia ocellata. Using a colorigenic substrate, the biochemical properties of this enzyme were studied and its activity was compared to the homologous one in CSs from the human parasite Schistosoma mansoni. The specific serine protease activity was always 2- to 3-fold higher in CSs from T. ocellatacompared to S. mansoni. The enzyme has its optimal activity at pH 10.5, is Ca2+-dependent (inhibition with EDTA) and… Show more

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Cited by 24 publications
(18 citation statements)
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“…However, this observation was not supported by Skelly and Shoemaker (2001). Bahgat and Ruppel (2002) reported on a comparison of S. mansoni elastase and a serine protease from Trichobilharzia ocellata. Their physicochemical properties were similar, both occurred as a doublet around 28 kDa in zymographic gels.…”
Section: Introductioncontrasting
confidence: 49%
“…However, this observation was not supported by Skelly and Shoemaker (2001). Bahgat and Ruppel (2002) reported on a comparison of S. mansoni elastase and a serine protease from Trichobilharzia ocellata. Their physicochemical properties were similar, both occurred as a doublet around 28 kDa in zymographic gels.…”
Section: Introductioncontrasting
confidence: 49%
“…This activity was linked with an orthologue of a chymotrypsin-like serine peptidase, named cercarial elastase and characterized from S. mansoni and S. haematobium cercariae. A protein on blots of T. szidati cercarial secretions as well as in histological sections of penetration glands immunologically cross-reacted with antibodies against elastases of S. mansoni and S. haematobium (183,184). However, in another study, the reaction of antibodies raised against elastase of S. mansoni was observed neither with the penetration glands of T. szidati nor with the cercarial secretions on Western blots (180).…”
Section: Vertebrate Host Finding and Penetrationmentioning
confidence: 87%
“…As is obvious from the nature of these substrates, none is specific for metalloproteinases utilizing collagen as a substrate. Gelatin, for example, is a substrate for MMP-2 (also called gelatinase A) [19,20] and is hydrolysed by elastase as well [21]. We have attempted to develop a zymogrambased method which can detect extremely low levels of collagenase, using collagen as the bait substrate.…”
mentioning
confidence: 99%
“…2). After the run was over, the gel was washed twice with distilled water and incubated with 20 mL of collagen solution (4 mg/mL), 8 mL of 0.05 M sodium phosphate (which is approximately 0.01 M in the final volume) and 28 mL of 1 M Ca 21 (which is 0.001 M Ca 21 in the final volume) for different intervals of time at 377C with shaking after which it was stained and destained.…”
mentioning
confidence: 99%
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