Table 1 of Srivastava, Mol Vis 2008; 14:1872-1885.

Table 1. Dissociation of proteinase activity from α-crystallin fraction.



Detergents concentration

Type		 Proteinase
activity
(e.u./ml)*
Sodium deoxycholate (1%) Anionic 1.04
Sodium dodecyl sulfate (0.1%) Anionic 1.05
Triton X-100 (0.1%) Non-ionic 0.5
Octyl-β-D-glucopyranoside (0.2%) Non-ionic 0.8
CHAPS (0.2%) Zwitterion 1.05

The proteinase activity was determined following detergent treatment of α-crystallin fraction. The asterisk indicates that proteinase activity is expressed as e.u./ml with BAPNA as a substrate. One e.u. is defined as the release of 1 nm/h of p-nitroanilide from BAPNA. Proteinase activity was determined by detergent treatment of the α-crystallin fraction followed by size-exclusion HPLC using a TSK G-3000 PW XL column.

Srivastava, Mol Vis 2008; 14:1872-1885. http://www.molvis.org/molvis/v14/a222

©2008 Molecular Vision http://www.molvis.org/molvis/

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