Abstract
Unfolding profiles of two calcium‐binding lysozymes, equine milk lysozyme and pigeon egg‐white lysozyme, were obtained by circular dichroism and proton NMR measurements. Equine lysozyme unfolds through a stable molten globule intermediate. The molten globule of equine lysozyme was characterized as more ordered than that of bovine α‐lactalbumin. On the other hand, pigeon lysozyme unfolds by a two‐state mechanism and the intermediate could not be observed in guanidine or thermal unfolding, the same as with conventional non‐calcium‐binding lysozymes. Thus, from the point of view of the unfolding profile, equine lysozyme belongs to the group of α‐lactalbumin, but pigeon lysozyme belongs to the conventional lysozyme group.
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Dates
Type | When |
---|---|
Created | 15 years ago (Aug. 9, 2010, 5:48 p.m.) |
Deposited | 1 year, 9 months ago (Oct. 25, 2023, 8:44 p.m.) |
Indexed | 1 month, 2 weeks ago (July 4, 2025, 7:48 a.m.) |
Issued | 32 years, 6 months ago (Feb. 1, 1993) |
Published | 32 years, 6 months ago (Feb. 1, 1993) |
Published Online | 16 years, 7 months ago (Jan. 12, 2009) |
Published Print | 32 years, 6 months ago (Feb. 1, 1993) |
@article{NITTA_1993, title={Comparative study of the stability of the folding intermediates of the calcium‐binding lysozymes}, volume={41}, ISSN={0367-8377}, url={http://dx.doi.org/10.1111/j.1399-3011.1993.tb00121.x}, DOI={10.1111/j.1399-3011.1993.tb00121.x}, number={2}, journal={International Journal of Peptide and Protein Research}, publisher={Wiley}, author={NITTA, KATSUTOSHI and TSUGE, HIDEAKI and IWAMOTO, HIROSHI}, year={1993}, month=feb, pages={118–123} }