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Extra resources for Vitamins and Coenzymes Part D
Example text
58, 563 (1974). 7 H. Nakagawa and A. Asano, J. Biochem. (Tokyo) 68, 737 (1970). 8 M. Nishikimi, B. M. Tolbert, and S. Udenfriend, Arch. Biochem. Biophys. 175, 427 (1976). 26 ASCORBIC ACID [4] fication are carded out at 0 - 4 °. 25 M sucrose by use of a Polytron homogenizer (Kinematica GmbH, Lucerne, Switzerland) and the homogenate is centrifuged for 15 min at 10,000 g. 4) and stored at - 2 0 °. Step 2. Tryptic Digestion. 3 mg/ml) and 1 mM EDTA, and are stirred gently overnight at 4 ° under nitrogen.
2a The r e m o v a l o f the c o p p e r f r o m the oxidase protein, and the simultaneous reduction of the disulfide bonds results in an a p o e n z y m e of lower structural stability than the holooxidase. 6 Reconstitution of a fully active oxidase from the inactive a p o e n z y m e involves the oxidative conversion of - S H groups to disulfide bonds. 79. 6 The colorless a p o a s c o r b a t e oxidase does not a b s o r b in the visible region. 2° The m a x i m u m specific activity values (units per milligram of protein or units per m i c r o g r a m of copper) of the reconstituted oxidase are essentially the same as those of the native holoascorbate oxidase.
Nishikimi, B. M. Tolbert, and S. Udenfriend, Arch. Biochem. Biophys. 175, 427 (1976). b Protein concentration was determined by the Lowry method, except for the preparation from hydroxyapatite column which was determined by the fluorescamine method. Step 7. Hydroxyapatite Chromatography. 5 cm) which has previously been equilibrated with the a b o v e p h o s p h a t e buffer. 4% Brij 35. 5 ml are collected, and those containing activity are c o m b i n e d and concentrated by ultrafiltration with a Diaflo m e m b r a n e PM 30.