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pubmed-article:1898866pubmed:abstractTextThe interaction between domain AB and domains CD*EF of pike parvalbumin III has been studied by intrinsic fluorescence spectroscopy. In the presence of Ca2+ ions, parvalbumin fragment 38-108 containing two calcium binding sites interacts with the short peptide 1-37 with association constant 10(5.3 +/- 0.5) M-1. Removal of Ca2+ ions results in the disappearance of the interaction. The affinity of the complex of the two fragments for calcium is 50-times higher than the affinity of the isolated fragment 38-108, but slightly lower than that of the intact protein.lld:pubmed
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pubmed-article:1898866pubmed:articleTitleNoncovalent complex between domain AB and domains CD*EF of parvalbumin.lld:pubmed
pubmed-article:1898866pubmed:affiliationInstitute of Biological Physics, U.S.S.R. Academy of Sciences, Pushchino, Moscow region.lld:pubmed
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