Skip to content
2000
Volume 15, Issue 10
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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.

Loading

Article metrics loading...

/content/journals/ppl/10.2174/092986608786071193
2008-10-01
2025-05-07
Loading full text...

Full text loading...

/content/journals/ppl/10.2174/092986608786071193
Loading

  • Article Type:
    Research Article
Keyword(s): Bid; Caspase-2; caspase-8; pH; procaspase-7; salt
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test