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Dissociation kinetics of parvalbumin complexes with calcium and magnesium ions were studied by means of stopped-flow method employing intrinsic protein fluorescence registration. In the temperature range from 10 to 30 degrees C the kinetic curves of Ca2+ and Mg2+ dissociation are best fitted with a sum of two exponential terms, each term is ascribed to a(More)
The binding of Ca+ to whiting parvalbumin has been studied by intrinsic (tryptophan) protein fluorescence. It has been shown that parvalbumin can exist in three states, which are interpreted as the protein without Ca2+ (P), with one bound Ca2+ (PC) and with two bound Ca2+ (CPC). The spectra of the states have been identified and the protein fluorescence(More)
On the basis of parvalbumin property to change Ca2+-binding constant within the pH-region from approxim-tely 7 to approximately 8 a hypothesis that parvalbumins are pH-regulated Ca2+-depot in muscles has been stated. The addition of parvalbumin to native actomysin complex at pH approximately 7 in the presence of ATP and Ca2+ results in partial inhibition of(More)
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