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α-Mannosidase as a Zinc-dependent Enzyme

Nature volume 218, pages 91–92 (1968)Cite this article

Abstract

CADMIUM has been reported to have a teratogenic effect in the golden hamster1, which is reversed by zinc. This prompts us to draw attention to our recent observation2 that zinc is an essential component of α-mannosidase. The active zinc–protein complex is readily dissociable at pH 5, the pH of optimum enzyme activity and the zinc ion can be displaced by cadmium, cobalt and other bivalent ions, with almost complete loss of enzyme activity (Fig. 1). These observations apply equally to the enzyme from rat epididymis3,4, jack bean meal5 and the limpet, Patella vulgata6.

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Authors and Affiliations

  1. Rowett Research Institute, Bucksburn, Aberdeen

    SYBIL M. SNAITH & G. A. LEVVY

Authors
  1. SYBIL M. SNAITH
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  2. G. A. LEVVY
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SNAITH, S., LEVVY, G. α-Mannosidase as a Zinc-dependent Enzyme. Nature 218, 91–92 (1968). https://doi.org/10.1038/218091a0

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