[pH-dependence of kinetic parameters in the superprecipitation reaction and ATPase activity of myometrial actomyosin].
The investigation of pH-dependence of superprecipitation reaction and ATPase activity of myometrium actomyosin in the interval of pH 5.5-8.0 has detected cupola-shaped curves with maximal activity of both processes by pH 6.5. On the basis of calculating the constants of ionization it was supposed that in the case of actomyosin ATPase imidazole groups of two histidins had an essential role in reaction of ATP hydrolysis and in superprecipitation process--imidazol group of histidine and carboxyl group of asparagin acid. The investigation of [ATP]- and [Mg2+]-dependence of superprecipitation reaction by pH 6.0, 6.5 and 7.0 has demonstrated different pH-sensitiveness of Michaelis constants and maximal speeds relatively Mg2+ and ATP for both processes. It was shown that pH-optimum of ATPase activity of myometrium actomyosin coincided with maximal affinity of actomyosin with ATP and Mg2+ while as for superprecipitation reaction the correlation between value of process by certain pH and affinity with ATP and Mg2+ was not detected.
Labyntseva
R D
RD
O.V. Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv.
Ul'nenko
T V
TV
Kosterin
S O
SO
D000205:Actomyosin / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005260:Female; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D009215:Myometrium / Q000201:enzymology / Q000378:metabolism*; D013552:Swine
D000255:Adenosine Triphosphate; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D008274:Magnesium