Abstract
The activity of caspase-2 was examined under varying biochemical conditions with the synthetic and protein substrates, Bid and procaspase-7. The results indicate that it was largely influenced by pH which might be one reason behind the inconsistency for the cleavage of its established substrates during caspase-2-induced apoptosis.
Protein & Peptide Letters
Title: Efficient Cleavage of Bid and Procaspase-7 by Caspase-2 at Lower pH
Volume: 15 Issue: 10
Author(s): Pratap Karki, Giri Raj Dahal, Song Yub Shin, Jung Sup Lee, Byungyun Cho and Il-Seon Park
Affiliation:
Keywords: Caspase-2, caspase-8, pH, salt, Bid, procaspase-7
Abstract: The activity of caspase-2 was examined under varying biochemical conditions with the synthetic and protein substrates, Bid and procaspase-7. The results indicate that it was largely influenced by pH which might be one reason behind the inconsistency for the cleavage of its established substrates during caspase-2-induced apoptosis.
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Cite this article as:
Karki Pratap, Dahal Raj Giri, Shin Yub Song, Lee Sup Jung, Cho Byungyun and Park Il-Seon, Efficient Cleavage of Bid and Procaspase-7 by Caspase-2 at Lower pH, Protein & Peptide Letters 2008; 15 (10) . https://dx.doi.org/10.2174/092986608786071193
DOI https://dx.doi.org/10.2174/092986608786071193 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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