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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Cloning and characterization of Schistosoma mansoni fructose-1,6-bisphosphate aldolase isoenzyme.

A Schistosoma mansoni cercarial cDNA expression library, constructed in lambda gt11, was screened using the IgG fraction of sera taken from rabbits vaccinated with irradiated cercariae. A positive cDNA clone (1,431 base pairs) was selected and characterized. The amino acid sequence predicted from the cDNA sequence identified a polypeptide of 363 amino acids that showed significant homology to different family members of the enzyme fructose-1,6-bisphosphate aldolase (EC 1.4.2.13). The identity was 66% and 65% with human C and A isoenzymes, respectively. Active sites and substrate-binding determinant analysis suggest that the isolated enzyme in terms of function resembles type A aldolase. The recombinant protein expressed in the vector pGEX-2T was found to be active enzymatically. Antibodies raised against the purified recombinant protein recognized a 40-kDa band in extracts from cercariae, schistosomula (5 and 25 days), adult worms, and eggs. Using immunocytochemistry, aldolase localized to the tegumental region of the adult worms.[1]

References

  1. Cloning and characterization of Schistosoma mansoni fructose-1,6-bisphosphate aldolase isoenzyme. El-Dabaa, E., Mei, H., El-Sayed, A., Karim, A.M., Eldesoky, H.M., Fahim, F.A., LoVerde, P.T., Saber, M.A. J. Parasitol. (1998) [Pubmed]
 
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