Letter | Published:

The Enzyme System Transferring the Amino-Group of Aspartic Acid

Nature volume 143, pages 603604 (08 April 1939) | Download Citation

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Abstract

I HAVE, in recent communications1,2, described a method for the preparation of a purified enzyme from muscle tissue, catalysing the reversible transfer of amino nitrogen from glutamic acid to monocarboxylic α-ketoacids3. The enzyme preparation is inactive with regard to the Umaminierung, or ‘trans-amination’ of aspartic acid, whereas this process is readily effected by the original muscle pulp4. I have since been successful in obtaining from muscle tissue, by means of a modified purification scheme to be described in detail elsewhere, enzyme preparations catalysing the transamination of aspartic acid at a considerable rate in the presence of a thermostable activator, or coenzyme, contained in tissue extracts.

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References

  1. 1.

    , Biochimia (Moscow), 3, 693 (1938).

  2. 2.

    C.R. Acad. Sci. U.R.S.S., 21, No. 1–2, 72 (1938).

  3. 3.

    and , Enzymologia, 2, 129 (1937).

  4. 4.

    , Biochimia, 4, No. 2 (1939) (in the Press).

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Author information

Affiliations

  1. Laboratory of Oxidation-Reduction Processes, Department of Metabolic Research, Viem, Moscow. Feb. 15.

    • M. G. KRITZMANN

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DOI

https://doi.org/10.1038/143603a0

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