Cloning and Characterization of Schistosoma mansoni Fructose-1,6-Bisphosphate Aldolase Isoenzyme
| Autor: | Fawzia A. Fahim, A. El-Sayed, Philip T. LoVerde, Amr M. Karim, Mohamed Saber, Ehab El-Dabaa, H. M. Eldesoky, H. Mei |
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| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
Aldolase A Fructose-bisphosphate aldolase Biology Molecular cloning biology.organism_classification Molecular biology Amino acid law.invention chemistry Biochemistry law Complementary DNA parasitic diseases biology.protein Recombinant DNA Parasitology Schistosoma mansoni Peptide sequence Ecology Evolution Behavior and Systematics |
| Zdroj: | The Journal of Parasitology. 84:954 |
| ISSN: | 0022-3395 |
| DOI: | 10.2307/3284627 |
| Popis: | A Schistosoma mansoni cercarial cDNA expression library, constructed in Xgtl 1, 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 actie 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. |
| Databáze: | OpenAIRE |
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