Abstract
The hemolytic lectin CEL-III and its site-directed mutants were expressed in Escherichia coli cells. Replacement of the valine clusters in domain 3 with alanine residues led to increased self-oligomerization in solution and higher hemolytic activity. The results suggest the involvement of these valine clusters in CEL-III oligomerization and hemolytic activity.
Keywords: Cucumaria echinata, hemolysin, lectin, oligomerization, site-directed mutagenesis
Protein & Peptide Letters
Title: Roles of the Valine Clusters in Domain 3 of the Hemolytic Lectin CEL-III in Its Oligomerization and Hemolytic Abilities
Volume: 16 Issue: 4
Author(s): Keigo Hisamatsu, Hideaki Unno, Shuichiro Goda and Tomomitsu Hatakeyama
Affiliation:
Keywords: Cucumaria echinata, hemolysin, lectin, oligomerization, site-directed mutagenesis
Abstract: The hemolytic lectin CEL-III and its site-directed mutants were expressed in Escherichia coli cells. Replacement of the valine clusters in domain 3 with alanine residues led to increased self-oligomerization in solution and higher hemolytic activity. The results suggest the involvement of these valine clusters in CEL-III oligomerization and hemolytic activity.
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Cite this article as:
Hisamatsu Keigo, Unno Hideaki, Goda Shuichiro and Hatakeyama Tomomitsu, Roles of the Valine Clusters in Domain 3 of the Hemolytic Lectin CEL-III in Its Oligomerization and Hemolytic Abilities, Protein & Peptide Letters 2009; 16 (4) . https://dx.doi.org/10.2174/092986609787848054
DOI https://dx.doi.org/10.2174/092986609787848054 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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