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Zn2+ binding to cardiac calsequestrin.

S Baksh·C Spamer·K Oikawa·W D McCubbin·C Heilmann·C M Kay·M Michalak
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Abstract

Zn2+ binding to canine cardiac calsequestrin was investigated using the Zn2+ specific fluorescence dye salicylcarbohydrazone (SACH), 65Zn2+ overlay and Zn(2+)-IDA chromatography. Cardiac calsequestrin binds approximately 200 moles of Zn2+/mole of protein with the Kd = 300 microM. Zn2+ binding to calsequestrin was further confirmed by 65Zn2+ overlay and Zn(2+)-dependent aggregation of the protein. However, calsequestrin did not bind to a Zn(2+)-IDA-agarose column, indicating that histidine residues may not be involved in Zn2+ binding to the protein. Circular dichroism revealed only minor Zn(2+)-dependent conformational changes in calsequestrin. We conclude that calsequestrin is a Ca(2+)- and Zn(2+)-binding protein and that Zn2+ may modulate the structure and function of the protein.

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AnimalsCalsequestrinChromatography, AffinityCircular DichroismDogsFluorescent DyesMuscle, SkeletalMyocardiumProtein BindingProtein ConformationRatsSpectrophotometry, UltravioletZincJournal ArticleResearch Support, Non-U.S. Gov't

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S Baksh, C Spamer, K Oikawa, W D McCubbin, C Heilmann, C M Kay, M Michalak. 1995-04-06. Zn2+ binding to cardiac calsequestrin.. https://doi.org/10.1006/bbrc.1995.1504

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