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Purification of Glyoxalase I From Onion Bulbs and Molecular Cloning of Its cDNA

Purification of Glyoxalase I From Onion Bulbs and Molecular Cloning of Its cDNA

Mohammad Anwar Hossain, Masayuki Fujita

Biosci Biotechnol Biochem. 2009 Sep;73(9):2007-13.

PMID: 19734676

Abstract:

Glyoxalase I was highly purified from onion bulbs by DEAE-cellulose, hydroxyapatite, and S-hexylglutathione-agarose column chromatography. With 356 micromol min(-1) mg(-1) protein, the specific enzymatic activity of the purified enzyme is the highest reported to date in plants. The purified enzyme showed a single major band with a relative molecular mass of approximately 25,000 on SDS-PAGE. A cDNA encoding glyoxalase I was cloned and sequenced. Sequence comparison suggested that it is to be classified as a short-type glyoxalase I. The expression pattern of glyoxalase I in healthy onion plants and responses to various stresses were examined by Western blotting. Glyoxalase I exists at high concentration in roots, young bulbs, mature bulbs, and mature leaves, the highest concentration being in mature bulbs. Up-regulation of glyoxalase I and glyoxalase II enzyme activities were observed in response to various stresses, and an increase in Gly I protein was also seen by immunoblotting. Our results suggest an important role of the glyoxalase I gene in the plant abiotic stress response.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42410999	S-Hexylglutathione-Agarose			Price

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