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d(-)-Lactate dehydrogenase from Allomyces

Partial purification and allosteric properties

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Summary

d(-)-lactate dehydrogenase from hybrid male strain of Allomyces has been partially purified.

The enzyme shows multiple binding sites for NADH. It obeys Michaelis-Menten kinetics for pyruvate. The inhibition of the enzyme activity by ATP is of mixed type. ADP is not an allosteric inhibitor of the enzyme. AMP and cyclic 3′,5′-AMP do not affect the enzyme. NAD+ acts as a product inhibitor.

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Authors and Affiliations

  1. Laboratoire de Microbiologie, Département de Biologie végétale, Université de Genève, Genève, Switzerland

    K. Purohit & G. Turian

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  1. K. Purohit
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  2. G. Turian
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Purohit, K., Turian, G. d(-)-Lactate dehydrogenase from Allomyces . Archiv. Mikrobiol. 84, 287–300 (1972). https://doi.org/10.1007/BF00409078

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  • DOI: https://doi.org/10.1007/BF00409078

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