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. 1997 Apr 15;94(8):3576–3578. doi: 10.1073/pnas.94.8.3576

Table 1.

Batchwise renaturation of cyclophilin A on mini-chaperone-agarose gels

Gel type Protein yield, % Activity yield, % Specific activity relative to “pure” native, %
GroEL(191–345)-Ni-NTA-agarose 84 98 103
GroEL(191–376)-Ni-NTA-agarose 81 105 115
GroEL(191–345)-agarose 87 125 126
HSA-agarose (control)* 84 33 35
Ethanolamine-agarose (control) 80 25 28
Agarose (control) 72 17 20
Native cyclophilin (control) 88§

Cyclophilin activity was measured in the supernatant as described (12). 

*

Human serum albumin (HSA) was covalently linked to CNBr-activated agarose. 

CNBr-activated agarose was coupled to ethanolamine. 

NTA-agarose after removal of the Ni from Ni-NTA agarose. 

§

The sample prior to denaturation had 88% of the specific activity of the highest activity of native cyclophilin previously obtained in this laboratory.