期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 73, 期 9, 页码 2007-2013出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90194
关键词
glyoxalase I; Allium cepa; enzyme purification; cDNA cloning; abiotic stress response
Glyoxalase I was highly purified from onion bulbs by DEAE-cellulose, hydroxyapatite, and S-hexylglutathione-agarose column chromatography. With 356 mu mol 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.
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