Purification of a cathepsin L-like proteinase secreted by adult Fasciola hepatica
Data(s) |
01/11/1993
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Resumo |
A cysteine proteinase released in vitro by Fasciola hepatica was purified to homogeneity by Sephacryl S-200 gel filtration chromatography followed by QAE-Sephadex chromatography. The purified enzyme resolves as a single band with an apparent molecular size of 27 kDa on reducing SDS-polyacrylamide gel electrophoresis; however, under non-reducing conditions it migrates as multiple bands, each with enzymatic activity, in the apparent molecular size range 60-90 kDa. The sequence of the first 20 N-terminal amino acids of the enzyme shows considerable homology with cathepsin L-like proteinases. Immunolocalisation studies revealed that the cathepsin L-like proteinase is concentrated within vesicles in the gut epithelial cells of liver fluke. |
Identificador | |
Idioma(s) |
eng |
Direitos |
info:eu-repo/semantics/restrictedAccess |
Fonte |
Smith , A M , Dowd , A J , McGonigle , S , Keegan , P S , Brennan , G , Trudgett , A & Dalton , J P 1993 , ' Purification of a cathepsin L-like proteinase secreted by adult Fasciola hepatica ' Molecular and Biochemical Parasitology , vol 62 , no. 1 , pp. 1-8 . |
Palavras-Chave | #Amino Acid Sequence #Animals #Cathepsin L #Cathepsins #Cattle #Chromatography, Gel #Chromatography, Ion Exchange #Cysteine Endopeptidases #Endopeptidases #Enzyme Precursors #Fasciola hepatica #Humans #Immunoblotting #Immunohistochemistry #Molecular Sequence Data #Rats #Sequence Homology, Amino Acid #Species Specificity |
Tipo |
article |