Please use this identifier to cite or link to this item:
|Title:||The role of cationic amino acid residues in the lethal activity of stonustoxin from stonefish (Synanceja horrida) venom|
|Source:||Khoo, H.-E.,Chen, D.,Yuen, R. (1998-03). The role of cationic amino acid residues in the lethal activity of stonustoxin from stonefish (Synanceja horrida) venom. Biochemistry and Molecular Biology International 44 (3) : 643-646. ScholarBank@NUS Repository.|
|Abstract:||Stonustoxin (SNTX) is a two subunit pore-forming cytolytic protein purified from the venom of the stonefish (Synanceja horrida). SNTX also possesses lethal activity. Since cationic residues contribute significantly to the cytolytic activity of several pore-forming toxins, we examined the role of lysine and arginine residues in the lethal activity of SNTX. SNTX lost its lethal activity when the positively-charged side chains of lysine residues were converted to negatively-charged side chains upon succinylation. When the arginine residues were modified using 2,3-butanedione, SNTX also lost its lethal activity. However, the domains for cytolytic and lethal activity may not necessarily be the same.|
|Source Title:||Biochemistry and Molecular Biology International|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 14, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.