Title : Conformational changes induced by zinc and terbium binding to native bovine alpha-lactalbumin and calcium-free alpha-lactalbumin.

Pub. Date : 1984 Sep 10

PMID : 6469988






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Conformational changes induced by zinc and terbium binding to native bovine alpha-lactalbumin and calcium-free alpha-lactalbumin. Terbium lactalbumin alpha Bos taurus
2 Conformational changes induced by zinc and terbium binding to native bovine alpha-lactalbumin and calcium-free alpha-lactalbumin. Terbium lactalbumin alpha Bos taurus
3 Terbium at submillimolar concentrations appears to bind to the calcium site of apo bovine alpha-lactalbumin and stabilizes the N conformation (fluorescence criterion; Kronman, M. J., Sinha, S., and Brew, K. (1981) J. Biol. Terbium lactalbumin alpha Bos taurus
4 Millimolar concentrations of Zn2+ induce a time-dependent conformational change in both calcium-free and calcium-liganded alpha-lactalbumin to produce an "expanded A-like state" comparable to that seen with terbium at similar concentrations. Terbium lactalbumin alpha Bos taurus