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Zn2+ binding to cardiac calsequestrin.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1995 Apr 06; Vol. 209 (1), pp. 310-5. - Publication Year :
- 1995
-
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.
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 209
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 7726852
- Full Text :
- https://doi.org/10.1006/bbrc.1995.1504