Abstract
RECENTLY Currie1 reported the strong adsorption of purine bases on precipitated protein. In spite of repeated washings with 8 per cent perchloric acid, only 30–40 per cent of the added quantity of xanthine, hypoxanthine and uric acid was recovered. The determination of the bases was carried out enzymatically with xanthine oxidase. As perchloric acid is at present being used as the standard method for deproteinization much of the work concerning the metabolism of purine derivatives would, as a result, be incorrect2–4.
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References
Currie, R., Nature, 205, 1212 (1965).
Gerlach, E., Deuticke, B., and Dresibach, R. H., Pflügers Archiv., 278, 296 (1963).
Thorn, W., and Busch, E. W., Biochem. Z., 339, 112 (1963).
Hutchison, W. C., and Munro, H. N., Analyst, 86, 768 (1961).
Busch, E. W., and Takriti, N., Angewandte Chemie, 77, 1080 (1965).
Reid, E., and Stevens, B. M., Biochem. J., 68, 367 (1958).
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BUSCH, EW., VON BOBRCKE, IM. Quantitative Determination of Purine Derivatives in the Presence of Denatured Protein. Nature 210, 631 (1966). https://doi.org/10.1038/210631a0
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DOI: https://doi.org/10.1038/210631a0
