Protein SB 431542 was improved by mutation of conserved homing endonuclease domain residues in the inteins, particularly for inteins two and three (data not shown). This is consistent with the results found in a study of the in vitro endonuclease activity of inteins two and three [8].
Splicing activity of intein one
Fig. 2.
Splicing and cleavage reactions of HRIR1GST and mutants. (A) SDS–PAGE analysis of about 1 μg of protein per lane. (B) Western blot using about 1.5 μg per lane, detected with primary antibody directed against GST.
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Splicing activity of white blood cell intein two
Fig. 3.
Splicing and cleavage reactions of HRIR2GST and mutants. (A) SDS–PAGE analysis of about 1 μg of protein per lane. (B) Western blot using about 1.5 μg per lane, detected with primary antibody directed against GST.
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Splicing activity of intein three
Fig. 4.
Splicing and cleavage reactions of HRIR3GST and mutants. (A) SDS–PAGE analysis of about 1 μg of protein per lane. (B) Western blot using about 1.5 μg per lane, detected with primary antibody directed against GST.
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Results show important individual variations both in terms
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