Partial purification and characterisation of the proteolytic enzymes of Fasciola gigantica adult worms.
The proteases of adult Fasciola gigantica whole worm were analysed by preparative isoelectric focusing and by gelatin-substrate gel electrophoresis at acidic and neutral pH (4.5 and 7.0). At least 15 bands of proteases were observed. These proteases had molecular weights ranging from 26 to 193 kDa and isoelectric points of 4.92-7.63. Protease-rich fractions were subsequently separated from whole worm preparation of the parasite by filtration in Sephacryl S-200. The proteases were able to digest bovine immunoglobulin G (IgG) and globin (derived from bovine haemoglobin) in vitro. The sizes of the proteases in these fractions were from 26 to 96 kDa, and they were inhibited by the protease inhibitors phenylmethylsulphonyl fluoride (PMSF), leupeptin and trasylol.
Fagbemi
B O
BO
Department of Veterinary Microbiology and Parasitology, University of Ibadan, Nigeria.
Hillyer
G V
GV
D000818:Animals; D002852:Chromatography, Ion Exchange; D004587:Electrophoresis, Agar Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D005209:Fasciola / Q000201:enzymology*; D007525:Isoelectric Focusing; D011480:Protease Inhibitors
D011480:Protease Inhibitors; D010450:Endopeptidases