Studies on Succinic Dehydrogenase

نویسنده

  • EDNA B. KEARNEY
چکیده

About 2 years ago the author reported that the activity of purified preparations of succinic dehydrogenase is enhanced by phosphate buffer (2). This enhancement was dependent upon the phosphate concentration and appeared to be relatively specific for phosphate, since other buffers, such as Tris,l imidazole, histidine, glycylglycine, and arsenate did not induce it (2, 3). Arsenate, in fact, interfered with the activation by phosphate in a competitive manner. Subsequent studies on the mechanism of the phosphate activation revealed that the activation was elicited by compounds capable of forming a complex with the active center of the enzyme and that it is characterized by a high energy of activation together with changes in the absorption spectrum and Michaelis constants of the enzyme suggestive of a configurational change in the protein (1). The present paper is a detailed account of these findings.

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تاریخ انتشار 2003