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题名: Purification and partial characterization of a protease associated with photosystem II particles
作者: Zhang, LX; Wang, J; Wen, JQ; Liang, HG; Du, LF
收录类别: SCIE ; BIOSIS
出版日期: 1995-12
刊名: Physiologia Plantarum
卷号: 95, 期号:4, 页码:591-595
出版者: MUNKSGAARD INT PUBL LTD
出版地: COPENHAGEN
英文摘要: A protease was extracted with 1 M NaCl from spinach (Spinacia oleracea L.) photosystem II (PSII) particles and purified through gel filtration and anion-exchange chromatography. SDS-polyacrylamide gel electrophoresis of the protease revealed a polypeptide with a molecular mass of 43 kDa. The activity of the purified protease was assayed using a 24 kDa water-soluble protein as substrate, visualized through SDS-PAGE. The protease even remained active in the presence of 0.1 and 0.2 M NaCl, although the degradation pattern changed, which indicated that the protease was different from that reported earlier by another group. The presence of 0.3 M NaCl was shown to Ire inhibitory. The protease was inhibited by 1,10-phenanthroline and EGTA-NaOH (pH 7.0), indicating that the metal ions are essential for activity and that the enzyme is a metal-protease. FTIR spectroscopy was used to examine the conformationally sensitive amide I' bands of the protease. The protease was observed to undergo spectroscopic changes that reflect the conformational changes that take place when Ca2+ is bound, which further confirms that the protease is a metal-protease.
关键词: enzyme activity ; FTIR ; PSII particles ; protease ; 24-kDa protein ; SDS-PAGE
作者部门: SICHUAN UNIV,DEPT BIOL,CHENGDU 610064,PEOPLES R CHINA
通讯作者: Zhang, LX (reprint author), LANZHOU UNIV,DEPT BIOL,LANZHOU 730000,PEOPLES R CHINA.
学科分类: Plant Sciences
文章类型: Article
语种: 英语
DOI: 10.1034/j.1399-3054.1995.950413.x
ISSN号: 0031-9317
WOS记录号: WOS:A1995TQ84100013
BIOSIS记录号: BCI:BCI199698686115
IR记录号: BCI:BCI199698686115
第一机构:
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内容类型: 期刊论文
URI标识: http://ir.lzu.edu.cn/handle/262010/115994
Appears in Collections:生命科学学院_期刊论文

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Recommended Citation:
Zhang, LX,Wang, J,Wen, JQ,et al. Purification and partial characterization of a protease associated with photosystem II particles[J]. Physiologia Plantarum,1995,95(4):591-595.
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