Letter | Published:

Reconstruction of Laccase from its Protein and Copper

Nature volume 162, pages 340341 (28 August 1948) | Download Citation



THE conception that oxidases are metallo-protein compounds in which the metal plays an essential part in the catalytic activity of the enzyme was introduced by Gabriel Bertrand1 in the course of his studies on laccase, the oxidizing enzyme present in the latex of the Indo-Chinese lacquer tree. As crude preparations of laccase contained an appreciable amount of manganese, Bertrand assumed that this metal forms the active part of the oxidase. A more recent study of this problem by Keilin and Mann2, based upon highly purified enzyme prepared on a large scale from the latex of different lacquer trees, produced evidence that the active metal is not manganese but copper. This view, however, was challenged by Didier Bertrand3, who claimed to have isolated an enzyme of higher activity which contained 0·15 per cent manganese and only 0·014 per cent copper.

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    , C.R. Acad. Sci., Paris, 118, 1215 (1894); 124, 1032 (1897); 124, 1355 (1897).

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    , and , Nature, 143, 23 (1939).

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    , Bull. Soc. Chim. biol., 28, 45 (1944); 29, 613 (1947).

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    , Biochem. Z., 299, 32 (1938).

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  1. Molteno Institute, University of Cambridge.



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