Isozymes of superoxide dismutase from Aloe vera.

Enzyme & protein Pub Date : 1996-01-01 DOI:10.1159/000468631
F Sabeh, T Wright, S J Norton
{"title":"Isozymes of superoxide dismutase from Aloe vera.","authors":"F Sabeh,&nbsp;T Wright,&nbsp;S J Norton","doi":"10.1159/000468631","DOIUrl":null,"url":null,"abstract":"<p><p>Extracts from the parenchymatous leaf gel and the rind of the Aloe vera plant (Aloe barbadensis Miller) were shown to contain seven electrophoretically-identifiable superoxide dismutases (SODs). The chromatographic elution profiles and the migration of these bands on native polyacrylamide gel electrophoresis (PAGE), for both the gel and rind, are quite similar. Two of these seven activities are insensitive to cyanide treatment, suggesting that they are mangano-SODs. The other five activities are sensitive to cyanide treatment, but insensitive to azide treatment and are presumed to be cupro-zinc SODs. All of the seven proteins appear to be homodimers with apparent native molecular masses centered at approximately 32 and 42 kD as indicated by SDS-PAGE and gel-filtration (FPLC) chromatography. The specific activities of SODs in the A. vera rind and gel are comparable to those of spinach leaves and of rabbit liver.</p>","PeriodicalId":11854,"journal":{"name":"Enzyme & protein","volume":"49 4","pages":"212-21"},"PeriodicalIF":0.0000,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468631","citationCount":"38","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme & protein","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000468631","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 38

Abstract

Extracts from the parenchymatous leaf gel and the rind of the Aloe vera plant (Aloe barbadensis Miller) were shown to contain seven electrophoretically-identifiable superoxide dismutases (SODs). The chromatographic elution profiles and the migration of these bands on native polyacrylamide gel electrophoresis (PAGE), for both the gel and rind, are quite similar. Two of these seven activities are insensitive to cyanide treatment, suggesting that they are mangano-SODs. The other five activities are sensitive to cyanide treatment, but insensitive to azide treatment and are presumed to be cupro-zinc SODs. All of the seven proteins appear to be homodimers with apparent native molecular masses centered at approximately 32 and 42 kD as indicated by SDS-PAGE and gel-filtration (FPLC) chromatography. The specific activities of SODs in the A. vera rind and gel are comparable to those of spinach leaves and of rabbit liver.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
芦荟超氧化物歧化酶同工酶。
结果表明,芦荟薄壁叶凝胶和芦荟外皮的提取物含有7种电泳可识别的超氧化物歧化酶(sod)。凝胶和果皮的色谱洗脱谱图和这些条带在天然聚丙烯酰胺凝胶电泳(PAGE)上的迁移非常相似。这7种活性中有2种对氰化物处理不敏感,表明它们是锰- sod。其他5种活性物对氰化物处理敏感,但对叠氮化物处理不敏感,推测为铜锌SODs。SDS-PAGE和凝胶过滤(FPLC)色谱显示,这7种蛋白都是同源二聚体,明显的天然分子质量中心约为32和42 kD。芦荟皮和凝胶中sod的比活性与菠菜叶和兔肝相当。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells. What structure and function of avian plasminogen activator and matrix metalloproteinase-2 reveal about their counterpart mammalian enzymes, their regulation and their role in tumor invasion. Proteases associated with invadopodia, and their role in degradation of extracellular matrix. Cooperation between matrix metalloproteinases and the plasminogen activator-plasmin system in tumor progression. Urokinase plasminogen activator as a predictor of aggressive disease in breast cancer.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1