Title of article
Thermal aggregation of hen egg white lysozyme: effect of polyamines
Author/Authors
Nobakht Motlagh Ghochani، Bi bi Fatemeh نويسنده Faculty of Paramedical Sciences , , Moosavi-Nejad، Seyedeh Zahra نويسنده Department of Biology, Alzahra University, Tehran, IR Iran, Tehran, IR Iran ,
Issue Information
فصلنامه با شماره پیاپی 15 سال 2013
Pages
6
From page
57
To page
62
Abstract
Protein aggregation is a serious problem for both biotechnology and cell biology. Diseases such as prion misfolding, Alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. Human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutations in the lysozyme gene. In this study, we investigated effect of small additives on the thermal aggregation of lysozyme. The main finding of this work is that multiple amine groups, spermine and spermidine, play pivotal roles in preventing the thermal aggregation of lysozyme. Our results showed that effect of spermine is more than spermidine.
Journal title
Journal of Paramedical Sciences (JPS)
Serial Year
2013
Journal title
Journal of Paramedical Sciences (JPS)
Record number
1150899
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