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Biochemical characterisation of the Li locus, which controls the activity of the cyanogenic β-glucosidase in Trifolium repens L



Biochemical characterisation of the Li locus, which controls the activity of the cyanogenic β-glucosidase in Trifolium repens L



Plant Molecular Biology 1(3): 169-181



The cyanogenic β-glucosidase (linamarase) was purified from white clover leaf tissue. The enzyme is a homodimer with a molecular weight of 105 300-103 400 daltons estimated from molecular exclusion chromatography. The effect of buffer ions on the pH optimum and charge properties of the enzyme are presented. A combination of molecular exclusion chromatography and CM cellulose ion exchange chromatography purified linamarase 16 fold to a single 62 000 dalton polypeptide on SDS polyacrylamide gel electrophoresis. This polypeptide represented about 5% of the total soluble leaf protein and can be seen as a prominent band in SDS polyacrylamide gel electrophoresis of crude leaf extracts from Li Li plants. Screening backcross progeny showed that extracts from li li plants, which have no linamarase activity, lack this 62 000 dalton polypeptide. Linamarase is the major glycoprotein in white clover leaf extracts which binds to Concanavalin A-Sepharose.

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Accession: 051800711

Download citation: RISBibTeXText

PMID: 24317961

DOI: 10.1007/bf00021030


Related references

Biochemical characterisation of the Li locus, which controls the activity of the cyanogenic beta-glucosidase in Trifolium repens L. White clover. Plant molecular biology: an international journal on fundamental research and genetic engineering(3): 169-181, 1982

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