Aggregated proteins accelerate but do not increase the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation.
作者： Jian Li , Zong Lin , Chih-chen Wang
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摘要: The effect of protein aggregates on the aggregation d-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) during unfolding and refolding has been studied. GAPDH follows a sigmoid course. presence increases rate but does not change extent final renaturation yield. It is suggested that function as seeds for via hydrophobic interaction with only folding intermediates destined to aggregate do affect distribution between pathways leading correct aggregation. Moreover, two different proteins interfere each other their simultaneous together in buffer. These findings provide insight into mechanism by which cells prevent against interference from proteins.
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