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- W2058737419 abstract "The NC-p65 cDNA is the first protease sequence cloned and described for Neospora caninum. The full length cDNA was isolated by 5'- and 3'-rapid amplification of cDNA ends (RACE). NC-p65 was composed of 865 amino acids with a predicted signal sequence, a proposed pro-domain, and an internal region of conserved repeats. Analysis of the deduced amino acid sequence revealed that this protein had homology to the serine proteases of the subtilisin-like superfamily (subtilases) and had a predicted active site made up of the catalytic residues, Asp 253, His 309. and Ser 484. Antibodies to recombinant NC-p65 recognized multiple bands on Neospora lysate immunoblots, but most intensely stained a 65 kDa band. When N. caninum proteins were purified with affinity resins specific for NC-p65 and analyzed for enzyme activity, a single specific band of reaction was observed on gelatin-saturated zymograms." @default.
- W2058737419 created "2016-06-24" @default.
- W2058737419 creator A5067241434 @default.
- W2058737419 creator A5074471954 @default.
- W2058737419 date "1999-10-01" @default.
- W2058737419 modified "2023-10-16" @default.
- W2058737419 title "Characterization of a cDNA encoding a subtilisin-like serine protease (NC-p65) of Neospora caninum" @default.
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- W2058737419 doi "https://doi.org/10.1016/s0166-6851(99)00127-9" @default.
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