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An electrophoretic study of the reversible binding of phosphate to ovalbumin
[摘要]

An electrophoretic method is described for the measurement of relatively weak interaction of ions with proteins, and illustrated with the ovalbumin-phosphate system in 0.1I buffers, pH6.1. Results indicate that under these conditions the interaction of a single dibasic phosphate ion with ovalbumin is described by an association constant of approx. 250M-1.

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