引用本文: |
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叶启腾,陈强,李春香.丝兰酶及其提取工艺的研究[J].广西科学,1995,2(4):6-10. [点击复制]
- Ye Qiteng,Chen Qiang,Li Chunxiang.Proteinases of Yucca and Their Extraction[J].Guangxi Sciences,1995,2(4):6-10. [点击复制]
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摘要: |
直接干燥丝兰叶表栅状组织获得粗酶。用硫酸铵分级盐析取得酶制剂,它的最适pH值为12。用有机汞作配基的琼脂糖凝胶4B柱分离出酶,聚丙烯酸胺凝胶电泳证明柱分离物为两个蛋白酶组分(YuccainⅠ、YuccainⅡ),簿层等电聚焦电泳证实这两个组分等电点分别为pH值9.77和pH值9.61,SDS电泳两个酶仅看到1条染色带,测得分子量为3万。它们的活性均依赖于巯基。 |
关键词: 丝兰酶 蛋白酶 分离 纯化 性质 |
DOI: |
投稿时间:1995-05-21 |
基金项目:国家自然科学基金 |
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Proteinases of Yucca and Their Extraction |
Ye Qiteng, Chen Qiang, Li Chunxiang
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(Guangxi Institute of Subtropical Crop, Yongwu Road, Nanning, Guangxi, 530001) |
Abstract: |
The crude enzyme was prepared by dehydration from palisade tissue. The enzyme preparation with an optimal pH of 12 was salted out with (NH4)2SO4. Two fractions obtained by chromatography on sepharose 4B column with organic mercury dentate were Yuccains Ⅰ, Ⅱ (proteinases) using electrophoresis in thin polyacrylamide gel. YuccainsⅠ, Ⅱ just showed one strip in SDSPAGE, and their molecular weithts were 30000 and isoelectric points were PH values of 9.77 and 9.61 respectively. Their activities were subject to the SH-. |
Key words: Yuccain proteinase extraction purification property |