Abstract

The flavoprotein adrenodoxin reductase was purified and examined. A method of preparing this enzyme is described. Certain assay modifications significantly enhanced its activity in reducing 2,6‐dichlorophenolindophenol. Following discelectrophoresis a bright yellow protein band resulted. The percentage amino acid composition of the protein is presented. Excitation of fluorescence took place at 290, 395 and 465 nm, while emission maxima were observed at 334, 523, 791 and 520 nm. Miniature electrofocusing of the purified enzyme showed that its isoelectric point is about pH 8.9.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call