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On a possible mechanism of the adenosinetriphosphatase of liver mitochondria



On a possible mechanism of the adenosinetriphosphatase of liver mitochondria



Biochimica et Biophysica Acta 29(2): 378-391



Treatment of mitochondria with dexycholate solutions of varying strengths results in a gradual and reproducible distegration of the mitochondria. This procedure also produced a characteristic release of Mg++ and of material absorbing maximally at 260 mu from the mitochondria. Curves relating DOC concentration to ATPase activity gave reproducibly a peak of DOC-activation, 2 peaks of DNP-activation, and 2 peaks of Mg++-activation. Digitonin and bilirubin produced similar effects of disintegration on the ATPase activity. The effects of EDTA on the Mg++ release and on the ATPase activities of DOC-treated mitochondria were noted. The various effects were interpreted to mean that it is bound Mg++ which participates in the enzyme activation. The effects of various inhibitors were tested on the DNP-activated ATPase of fresh mitochondria and on the Mg++-activated ATPase of DOC-treated mitochondria. Some compounds, p-chloromercuribenzoate, azide, guanidine, EDTA, AMP and ADP inhibited both activities to varying degrees. Other compounds, arsenate, amytal, oxidized dichlorophenol-indophenol. (DCPIP), methylene blue, and vitamin K3 inhibited to varying degrees only the DNP-activated ATPase. The reactions with the detergents and with the inhibitors were interpreted to mean that the DNP-activated ATPase reaction is a 2-step reaction, and that the Mg++-activated ATPase of aged or DOC-treated mitochondria involves a cleavage between these 2 steps. One of these reactions involves a postulated site inhibited by azide and guanidine, which the other reaction involves a site common to the respiratory chain and which is blocked in various degrees and modes by certain inhibitors affecting the respiratory chain, such as amytal, oxidized DCPIP, and methylene blue. A fuller outline of this interpretation is given. Using higher concentrations of DOC, the Mg++-activated ATPase could be concentrated in a fraction containing the succinoxidase activity and which had been previously identified as being derived from the mitochondrial membrane.

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Accession: 025141399

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PMID: 13572356

DOI: 10.1016/0006-3002(58)90197-5


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