Zn2+ binding to cardiac calsequestrin

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 cal...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1995-04, Vol.209 (1), p.310-315
Main Authors: Baksh, S, Spamer, C, Oikawa, K, McCubbin, W D, Heilmann, C, Kay, C M, Michalak, M
Format: Article
Language:English
Subjects:
Animals
Calsequestrin - chemistry
Calsequestrin - metabolism
Chromatography, Affinity
Circular Dichroism
Dogs
Fluorescent Dyes
Muscle, Skeletal - metabolism
Myocardium - metabolism
Protein Binding
Protein Conformation
Rats
Spectrophotometry, Ultraviolet
Zinc - metabolism
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1995.1504