Studies on photosystem I. I. Relationship of plastocyanin, cytochrome f and P700 |
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| Authors: | J N Siedow V A Curtis A San Pietro |
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| Affiliation: | Section of Biochemistry, Molecular and Cell Biology, and the Graduate School of Nutrition, Cornell University, Savage Hall, Ithaca, New York 14850 U.S.A. |
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| Abstract: | DEAE-Sephadex column chromatography now has been used for the final step in purification of d-amino acid oxidase apoenzyme. A specific enzymatic activity of 35–37 units/mg has been obtained for the pure holoenzyme. The purity has been established by disc and SDS gel electrophoreses and by sedimentation equilibrium. The molecular weight per enzyme monomer has been found to be 38,000 ± 1000. Each enzyme monomer binds one FAD and one benzoate with dissociation constants at 23 °C and pH 8.5 of 5.35 × 10?7m and 1.96 × 10?6m, respectively. The holoenzyme is more negatively charged than the apoenzyme at alkaline pH. The amino acid composition and some other physicochemical properties of the oxidase are reported. |
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| Keywords: | To whom reprint requests should be sent. |
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