Báo cáo khoa học: Characterization of native and recombinant A4 glyceraldehyde 3-phosphate dehydrogenase Kinetic evidence for conformation changes upon association with the small protein CP12
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A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was purified from the green algaChlamydomonas reinhardtii andwas alsooverexpressed inEscherichia coli. Bothpurified A4 tetramers of recombinant and native GAPDH were characterized for the first time. The pH optimum for both nativeandrecombinant enzymeswas close to7.8.ThepKsof theresidues involvedincatalysis indicate thatacysteineanda histidinemay take part in catalysis by chloroplast GAPDH, as is the case for glycolytic GAPDH.
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