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. 1968 Dec;110(4):663–670. doi: 10.1042/bj1100663

Purification and properties of α-d-mannosidase from jack-bean meal

Sybil M Snaith 1, G A Levvy 1
PMCID: PMC1187437  PMID: 4973951

Abstract

1. α-Mannosidase from jack-bean meal was purified 150-fold. β-N-Acetyl-glucosaminidase and β-galactosidase were removed from the preparation by treatment with pyridine. Zn2+ was added during the purification to stabilize the α-mannosidase. 2. At pH values below neutrality, α-mannosidase undergoes reversible spontaneous inactivation at a rate dependent on the temperature, the degree of dilution and the extent of purification. The enzyme is also subject to irreversible inactivation, which is prevented by the addition of albumin. 3. Reversible inactivation of α-mannosidase is accelerated by EDTA and reversed or prevented by Zn2+. Other cations, such as Co2+, Cd2+ and Cu2+, accelerate inactivation; an excess of Zn2+ again exerts a protective action, and so does EDTA in suitable concentration. 4. Neither Zn2+ nor EDTA has any marked effect in the assay of untreated enzyme. In an EDTA-treated preparation, however, Zn2+ reactivates the enzyme during assay. 5. It is postulated that α-mannosidase is a dissociable Zn2+–protein complex in which Zn2+ is essential for enzyme activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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