By Boschke F.L.

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I0- ,~ [NTP] 10-3 10-2 (M) E "-x E NTP I0o. SO 84 i0-, ' ...... i0-0 ....... ;b-, ....... ib-* ....... ib-" ' ...... ib-, ' Nop Fig. 13. Dependence on ATP and ITP concentration of calcium dependent phosphate liberation (a) and the corresponding nucleoside triphosphate synthesis on the concentration of ADP, IDP and GDP. 6 Binding of Low Affinity Phosphate Donors and Inorganic Phosphate The affinities of the transport protein for the nucleoside triphosphates ITP and GTP and the corresponding diphosphates deduced from the concentration dependence of either calcium-dependent phosphate liberation or phosphate incorporation during calcium efflux are at least 10 to 400 times lower than the affinity of the adenine nucleotides (Fig.

To facilitate the analysis, the reaction sequence will be dissected in its elementary steps whenever the analysis does not require the complete transport system. Partial reactions can most favourably be studied with modified preparations or the isolated transport protein. These preparations do not only provide simplicity but enable one to gain inside into the role of the various constituents of the system. 106M -1 by the purified ATPase, by the transport protein in the native membranes as well as by partially delipidated, reversibly inactivated membrane preparations 11s' 119, 173).

106 M- t for the affinity constant obtained by appropriate binding studies is 3 to I0 fold higher than those obtained by the indirect procedure. The rather complex dependence of the calcium activated ATPase on the concentration of ATP has been taken as an indication for the involvement of more than one class of ATP binding sites. 1/aM. The activity increase at 37 w. 1 mM and 10 mM s43' 164, 181) (Fig. 13). This kind of activity profile has been taken as an indication that we are dealing with negative cooperativity between two ATP binding sites.

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