BMB Reports

생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
권호 표지

Purification and Characterization of Glyoxalase I from Chlamydomonas reinhardtii

  • Hwang, Sun-Jun (Department of Biochemistry and Molecular Biology, Hanyang University) ;
  • Chai, Young-Gyu (Department of Biochemistry and Molecular Biology, Hanyang University)
  • 투고 : 1995.11.30
  • 발행 : 1996.07.31
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초록

Glyoxalase I (Ee 4.4.1.5, lactoylglutathione lyase) from Chlamydomonas reinhardtii was purified to homogeneity by ammonium sulfate fractionation, anion-exchange chromatography, hydrophobic interaction chromatography, and affinity chromatography on S-hexylglutathione agarose. The purified enzyme was judged to be homogeneous on SDS-PAGE, and consisted of a single polypeptide chain with a relative molecular weight of 24,000. The enzyme was most active at $40^{\circ}C$ and pH 7.5. It was catalytically most active with methylglyoxal as substrate. A number of properties of the Chlamydomonas glyoxalase I enzyme, such as substrate specificity, molecular mass, kinetic parameters, pi, metal ion effect, have been determined and compared with those reported for preparations from other sources. It had somewhat different characteristics from mammalian enzymes.

키워드

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