Letter | Published:

Isoenzymes of Lactate-dehydrogenase in Micro-organisms

Naturevolume 207pages783784 (1965) | Download Citation

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Abstract

IT is generally accepted that lactate-dehydrogenase (LDH) exists in more than one molecular species. LDH isoenzymes have been separated by (among other methods) using their eventual heat stability at 58° C (ref. 1). It has been shown that the LDH fraction prominent in heart muscle is more stable to heat than other fractions from, for example, liver tissue2. There is good correlation between this heat-stable isoenzyme and the fastest moving, anodal LDH I (nomenclature of Wieme3) in electrophoresis.

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References

  1. 1

    Latner, A. L., and Skillen, A. N., Proc. Assoc. Clin. Biochem., 2, 100 (1963).

  2. 2

    Plagemann, P. G. W., Gregory, K. F., and Wróblewski, F., Biochem. Z., 334, 37 (1963).

  3. 3

    Wieme, R. J., Lancet, i, 270 (1962).

  4. 4

    King, J., J. Med. Lab. Technol., 18, 168 (1961).

  5. 5

    Richterich, R., Schafroth, P., and Franz, H. E., Enzymol. Biol. Clin., 1, 114 (1961–62).

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  1. Research Institute for Hygiene, Ul.čsl.arm. 40, Bratislava, Czechoslovakia

    • J. KELLEN

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https://doi.org/10.1038/207783b0

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