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. 1991 Oct;97(2):786–792. doi: 10.1104/pp.97.2.786

Purification and Developmental Analysis of a Metalloendoproteinase from the Leaves of Glycine max 1

John S Graham 1, Jin Xiong 1, Jeffery W Gillikin 1
PMCID: PMC1081075  PMID: 16668467

Abstract

A metalloendoproteinase from leaves of soybean (Glycine max) has been purified 1160-fold to electrophoretic homogeneity. The native protein is monomeric with a molecular mass of 15 kilodaltons as estimated by gel filtration and 19 kilodaltons as estimated by denaturing gel electrophoresis. The enzyme has a pH optima of 8.0 to 9.0 using Azocoll as substrate. The proteolytic activity is susceptible to metal chelating agents and the inactivated enzyme can be restored to 69% of original activity by the addition of ZnCl2. Western analysis shows that a fraction of the soybean metalloendoproteinase is present within the extracellular space of older leaves. Soybean metalloendoproteinase 1 is the Azocollase A activity first described by Ragster and Chrispeels (Plant Physiol 64: 857-862; 1979).

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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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