By Donald B. McCormick, Lemuel D. Wright
The severely acclaimed laboratory regular, Methods in Enzymology, is without doubt one of the so much hugely revered courses within the box of biochemistry. considering that 1955, each one quantity has been eagerly awaited, usually consulted, and praised through researchers and reviewers alike. The sequence includes a lot fabric nonetheless proper today—truly an important booklet for researchers in all fields of existence sciences
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W. Perry, and A. A. Liebman, Carbohydr. Res. 47, 172 (1976). [6] THE PREPARATION OF L-ASEORBIC ACID [35S]2-SULFATE 41 acid (III) can be carried out more efficiently (74% yield after crystallization) with sulfur trioxide in dimethylformamide. Removal of the 5,6protective isopropylidene group is effected by passage of the labeled substrate (IV) through a column of D o w e x 50 (H +) ion-exchange resin, 2 a method that minimizes contamination of the product with inorganic sulfate. I° Procedure 5,6-O-Isopropylidene L-Ascorbic Acid.
630 (1965). 5 T. M. Chu and W. R. , Steroids 12, 309 (1968). 6 R. O. Mumma, A. J. Verlangieri, and W. W. Weber, Carbohydr. Res. 19, 127 (1971). METHODS IN ENZYMOLOGY, VOL. 62 Copyright © 1979 by Academic Press, Inc. All rights of reproduction in any form reserved. ISBN 0-12-181962-0 40 ASCORBIC ACID [6] tic solvent. Although other sulfating agents e have been used, these procedures frequently generated poor yields of amorphous products containing considerable amounts of inorganic sulfate. Improved procedures 7,s for the preparation of L-ascorbic acid 2-sulfate have been reported including the direct sulfation r of L-ascorbic acid, but these methods have been directed mainly at the synthesis of unlabeled material.
The enzyme obtained from the above purification procedure is homogeneous by the criteria of ultracentrifugal analysis and electrophoresis on polyacrylamide gel. Stability. Incubation of the purified enzyme (freshly prepared) at 80° for 10 min results in complete loss of activity. Enzyme solutions containing in the order of 10,000 units/ml or higher (3 mg or higher of enzyme protein per milliliter) retain about 80% of their activity after storage for 3 months at 4 °. Substrate Specificity. Ascorbate oxidase exhibits a high degree of specificity toward L-ascorbic acid and certain related compounds.
