-transparent.png){kind=logo}
Although native aequorin is highly susceptible to inactivation, apoaequorin is highly resistant to various processes of denaturation. Apoaequorin was inactivated only partially at a temperature of 95 degrees C or by treatments with 6 M-urea, 4 M-guanidine hydrochloride, 1 M-HCl and 1 M-NaOH. It was nearly completely inactivated in 85% ethanol or by heating at 95 degrees C in 2 M-(NH4)2SO4, but over 50% of apoaequorin activity was restored in both cases merely by dissolving the coagulated protein in 4 M-guanidine hydrochloride. In the reconstitution of aequorin, partially inactivated apoaequorin yielded more aequorin than expected from the activity of the partially inactivated apoaequorin used, suggesting that the process of reconstitution promotes the renaturation of denatured apoaequorin.
O Shimomura, and
A Shimomura
March 2001,
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
O Shimomura, and
A Shimomura
September 1988,
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
O Shimomura, and
A Shimomura
January 1993,
Proteins,
O Shimomura, and
A Shimomura
September 2022,
Photochemistry and photobiology,
O Shimomura, and
A Shimomura
November 1986,
Proceedings of the National Academy of Sciences of the United States of America,
O Shimomura, and
A Shimomura
November 1985,
Biochemistry,
O Shimomura, and
A Shimomura
April 1989,
Photochemistry and photobiology,
O Shimomura, and
A Shimomura
January 1989,
Proceedings of the National Academy of Sciences of the United States of America,
O Shimomura, and
A Shimomura
August 1992,
FEBS letters,
O Shimomura, and
A Shimomura
March 2007,
Biochemical and biophysical research communications,
