Abstract
Two distinct endopeptidases were detected histochemically in the cercariae ofDiplostomum pseudospathaceum: a serine proteinase occupying the ceca and a cysteine proteinase occupying the penetration glands. The former was relatively resistant to formaldehyde, required either Ca2+ or Mg2+ for its stability, and was sensitive to organic fluorophosphate inhibitors but insensitive to thiol-blocking agents. The latter enzyme required both reducing and divalent cation-complexing agents for its full activity and was sensitive to formaldehyde, thiolblocking agents, and diazonium salts. Both enzymes hydrolyzed a number ofN-blockedl-aminoacyl-, andN-blockedl-peptidyl-naphthylamides bearingl-arginine at the P1 subsite. The pH optima for hydrolysis of the substrates were 8.0 for the serine proteinase and 7.6 for the cysteine proteinase.
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Abbreviations
- TAPS :
-
N-tris(hydroxymethyl)methyl-3-aminopropanesulfonic acid
- MOPS :
-
3-(morpholino)-propanesulfonic acid
- EDTA :
-
ethylenediaminetetraacetic acid
- DTE :
-
dithioerythritol
- ZN :
-
benzyloxycarbonylpHMB sodiump-hydroxymercuribenzoate
- NEM :
-
N-ethylmaleimide
- DFP :
-
diisopropyl fluorophosphate
- PMSF :
-
phenylmethanesulfonyl fluoride
References
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This work was supported by research grant PB 6 6004 92 03 from the State Committee for Scientific Research.
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Moczoń, T. Histochemistry of proteinases in the cercariae ofDiplostomum pseudospathaceum (Trematoda, Diplostomatidae). Parasitol Res 80, 684–686 (1994). https://doi.org/10.1007/BF00932953
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DOI: https://doi.org/10.1007/BF00932953