Unfolding of chondroitinase ABC Ι is dependent on thermodynamic driving force by kinetically rate constant-amplitude compensation: A stopped-flow fluorescence study
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- 作者：S. Akram Shirdela ; Khosrow Khalifeha ; Bijan Ranjbarb ; Abolfazl Golestanic ; Khosro Khajehd ; khajeh@modares.ac.ir" class="auth_mail" title="E-mail the corresponding author ; khajeh_k@yahoo.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Chondroitinase ABC Ι ; Thermal stability ; Unfolding kinetics ; Stopped-flow ; Conformational change ; Limited proteolysis
- 刊名：Enzyme and Microbial Technology
- 出版年：2016
- 出版时间：November 2016
- 年：2016
- 卷：93-94
- 期：Complete
- 页码：200-206
- 全文大小：1425 K
文摘
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L701T, H700N and H700N/L701T variants of chondroitinase are more stable than the wild type.
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Conformationally stabilized mutants with slower inactivation rate are more resistant to tryptolytic digestion.
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Unfolding kinetics data indicate that chondroitinase ABC I unfolded via three different pathways.
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More population of stabilized mutants unfolded via slower unfolding phase.