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- W2016291266 abstract "Crystals of lobster holo-d-glyceraldehyde-3-phosphate dehydrogenase, grown in ammonium sulfate, were dialyzed against sodium citrate buffer at pH 6·2. This procedure caused two sulfate ions in each active center to be displaced by one bridging citrate ion. The position of these two ion sites can be associated with the terminal phosphate group of the substrate and the participating inorganic phosphate. The degree of occupancy by the sulfate ions is the same in all four subunits within experimental error." @default.
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- W2016291266 title "Anion binding sites in the active center of d-glyceraldehyde-3-phosphate dehydrogenase" @default.
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- W2016291266 doi "https://doi.org/10.1016/s0022-2836(76)80083-6" @default.
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