Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes.


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 alpha-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 alpha-lactalbumin, but pigeon lysozyme belongs to the conventional lysozyme group. Study holds ProTherm entries: 10366, 10367, 10368 Extra Details: Transition I calcium-binding lysozyme; alpha-lactalbumin; folding intermediate;,pigeon lysozyme; equine lysozyme

Submission Details

ID: fnniKHft3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Nitta K;Tsuge H;Iwamoto H,Int. J. Pept. Protein Res. (1993) Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes. PMID:8458685
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