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- W272299995 abstract "Terbium ion binds to calcium-free Limulus hemocyanin at pH 7.0 and 8.9, and promotes the aggregation of hemocyanin subunits, a phenomenon associated with calcium binding. An excitation maximum for the bound terbium at 293 nm and the results of treating the hemocyanin with N-bromosuccinimide indicate that energy transfer from tryptophan to the bound terbium is responsible for the enhancement of terbium fluorescence. At pH 8.9, addition of calcium to hemocyanin containing bound terbium results in only a partial loss of terbium fluorescence, suggesting heterogeneity in the terbium binding sites. Titration of hemocyanin with terbium also indicates multiple binding sites." @default.
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- W272299995 date "1981-06-01" @default.
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- W272299995 title "Terbium ion binding to Limuluspolyphemus hemocyanin" @default.
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- W272299995 doi "https://doi.org/10.1016/0006-291x(81)91966-5" @default.
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