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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 1998.1
- 수록면
- 235 - 240 (6page)
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초록· 키워드
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The myristoyl-acyl carrier protein (ACP) specific thioesterase from Iris tectorum was purified to a considerable homogeneity and characterized. The enzyme was eluted with a considerable stability by double-gradients using Triton X-100 and low ionic KCl or Na-phosphate through DEAE-52, Octyl-Sepharose, Q-Sepharose, and hydroxyapatite chromatoraphy. SDS-PAGE analysis showed a single band of 39 kDa. The native molecular weight was estimated to be 82 kDa by Sephacryl S-200 chromatography, indicating that the enzyme was a dimer. The thioesterase showed a chain-length specificity to myristoyl-ACP in preference to other-ACPs. The enzyme activity decreased by 1.0 mM myristate to about 27% of the original activity, whereas the remaining activity with decanoate was about 90%. The purified thioesterase was inhibited by myristoyl-CoA more than by myristate, suggesting that the myristoyl-AGP thiolesterase might be controlled by myristic acid and/or a subsequent product myristoyl-CoA. In addition, some biochemical characteristics of the enzyme were described.
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