HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science / Faculty of Science >
Peer-reviewed Journal Articles, etc >

Calcium-binding and structural stability of echidna and canine milk lysozymes

Files in This Item:
PS7_10.pdf5.6 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/7394

Title: Calcium-binding and structural stability of echidna and canine milk lysozymes
Authors: Kikuchi, M. Browse this author
Kawano, K. Browse this author →KAKEN DB
Nitta, K.3 Browse this author →KAKEN DB
Authors(alt): 新田, 勝利3
Issue Date: Oct-1998
Publisher: Cambridge University Press
Journal Title: Protein Science
Volume: 7
Issue: 10
Start Page: 2150
End Page: 2155
Abstract: For echidna and canine milk lysozymes, which were presumed to be the calcium-binding lysozymes by their amino acid sequences, we have quantitated their calcium-binding strength and examined their guanidine unfolding profiles. The calcium-binding constants of echidna and canine lysozymes were determined to be 8.6 x 10(6) M(-1) and 8.9 x 10(6) M(-1) in 0.1 M KCl at pH 7.1 and 20 C, respectively. The unfolding of decalcified canine lysozyme proceeds in the same manner as that of alpha-lactalbumin, through a stable molten globule intermediate. However, neither calcium-bound nor decalcified echidna lysozyme shows a stable molten globule intermediate. This unfolding profile of echidna lysozyme is identical to that of conventional lysozymes and pigeon egg-white lysozyme, avian calcium-binding lysozyme. This result supports the suggestion of Prager and Jolles (Prager EM, Jolles P. 1996. Animal lysozymes c and g: An overview. In: Jolles P, ed. Lysozymes: Model enzymes in biochemistry and biology. Basel-Boston-Berlin: Birkhauzer Verlag. pp 9-31) that the lineage of avian and echidna calcium-binding lysozymes and that of eutherian calcium-binding lysozymes diverged separately from that of conventional lysozymes.
Rights: Copyright © 1998 Cambridge University Press
Type: article
URI: http://hdl.handle.net/2115/7394
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 新田 勝利

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University