{"title":"Herbicide Action and Effects on Detoxification Processes","authors":"A. Dodge","doi":"10.1201/9781351070454-9","DOIUrl":"https://doi.org/10.1201/9781351070454-9","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77619206","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-07-22DOI: 10.1201/9781351070454-12
W. Van Camp, M. Van Montagu, D. Inzé
Superoxide dismutase was purified from pea (Pisum sativum L., cv. Wando) seeds and corn (Zea mays L., cv. Michigan 500) seedlings. The purified pea enzyme eluting as a single peak from gel exclusion chromatography columns contained the three electrophoreticaUy distinct bands of superoxide dismutase characterizing the crude extract. The purified corn enzyme eluted as the same peak as the pea enzyme, and contained five of the seven active bands found in the crude extract. The similar molecular weights and the cyanide sensitivities of these bands indicated that they are probably isozymes of a cupro-zinc superoxide dismutase. One of the remaining corn bands was shown to be a peroxidase. Superoxide dismutase accounted for 1.6 to 2.4% of the water-soluble protein in seedlings of corn, peas, and oats (Avena sativa L., cv. Au Sable). The superoxide dismutase activity per plant and per milligram water-soluble protein considerably increased during germination of oats and during greening and hook opening of peas. In a previous study, considerable amounts of SOD3 were found to be present in roots, shoots, seeds, and seed parts of oats, corn, and peas (4). Electrophoresis indicated multiple forms of the enzyme. Significant differences in quantity and forms of the enzyme were observed between species and between organs within a species. The objective of this study was to substantiate further the occurrence of the enzyme in higher plants and to examine the observed differences between species. For this purpose the enzyme was purified. Changes of SOD activity during seedling growth were also studied. MATERIALS AND METHODS Enzyme Purification. Unless otherwise stated, all operations were performed at 0 to 4 C. Dry pea seeds (Pisum sativum L., cv. Wando) were soaked in distilled H20 for about 15 hr. The resulting 1650 g wet weight was crushed with an electric mortar and pestle and homogenized with 1 liter of 0.1 M K2HPO4 in a Waring Blendor. The resulting pH was 7.5. After stirring, the slurry was filtered/squeezed through six layers of cheesecloth. The filtrate was centrifuged twice at 13000g for 30 min in a Sorvall RC2-B refrigerated centrifuge. The supernatant was subjected to the Tsuchihashi (chloroform-ethanol) treatment essentially as described by Weisiger and I Michigan Agricultural Experiment Station Journal Article No. 7765. 2 This paper represents part of the Ph.D. dissertation of C. N. G. Abbreviations: SOD: superoxide dismutase (EC 1 .15.1.1); NBT: pnitro blue tetrazolium chloride. Fridovich (10). None of the pea SOD enzymes is inactivated by this treatment. The supernatant was mixed with 0.25 volume of ethanol and 0.15 volume of chloroform and stirred for 15 min. It was then clarified by centrifugation at 13000g for 15 min. Chloroform that was separated out during centrifugation was removed by suction. The supernatant was decanted, solid K2HPO4 (20 g/l) was added, and the two phases were separated after 30 min. The less dense, ethanol-rich phase was c
从豌豆(Pisum sativum L.， cv.)中纯化超氧化物歧化酶。Wando)种子和玉米(Zea mays L.， cv。密歇根州500)幼苗。纯化后的豌豆酶在凝胶排斥层析柱上为单峰，其中包含粗提取物的三个不同的超氧化物歧化酶电泳带。纯化后的玉米酶与豌豆酶具有相同的峰，并且含有粗提取物中发现的7个活性带中的5个。相似的分子量和对氰化物的敏感性表明它们可能是铜锌超氧化物歧化酶的同工酶。剩下的玉米条带之一被证明是过氧化物酶。玉米、豌豆和燕麦(Avena sativa L.， cv.)幼苗中超氧化物歧化酶占水溶性蛋白质的1.6 ~ 2.4%。非盟貂)。单株超氧化物歧化酶活性和每毫克水溶性蛋白活性在燕麦发芽期和豌豆发芽期显著增加。在之前的一项研究中，在燕麦、玉米和豌豆的根、芽、种子和种子部分中发现了相当数量的SOD3(4)。电泳显示了该酶的多种形式。酶的数量和形式在物种之间和物种内的器官之间都有显著差异。本研究的目的是进一步证实该酶在高等植物中的存在，并检查所观察到的物种之间的差异。为此，对酶进行了纯化。研究了幼苗生长过程中SOD活性的变化。材料和方法酶纯化。除非另有说明，所有操作均在0 - 4℃下进行。Wando)在蒸馏水中浸泡约15小时。得到的1650g湿重用电动臼和杵粉碎，用1升0.1 M K2HPO4在Waring搅拌机中均质。所得pH值为7.5。搅拌后，浆料通过六层粗棉布过滤/挤压。滤液在Sorvall RC2-B冷冻离心机中13000g离心2次，离心30 min。上清液采用土桥(氯仿-乙醇)处理，基本按照Weisiger和密歇根农业实验站杂志第7765号文章的描述进行处理。2本文为c.n.g.博士学位论文的一部分。缩写:SOD:超氧化物歧化酶(EC 1.15.1.1);NBT:硝基蓝四氮氯化铵。Fridovich(10)。这种处理没有使豌豆SOD酶失活。将上清液与0.25体积的乙醇和0.15体积的氯仿混合，搅拌15分钟，13000g离心澄清15分钟，将离心过程中分离出的氯仿吸出。洗脱上清，加入固体K2HPO4 (20 g/l)， 30min后分离两相。收集密度较低、富含乙醇的相，冷冻后-15℃离心，吸力除去离心过程中分离出的氯仿，洗脱乙醇相。在搅拌的同时，将0.5体积的冷冻丙酮加入乙醇相。沉淀物经离心除去。在上清液中加入额外的丙酮(1.5体积)，收集第二次沉淀并在0.05 M K-phosphate (pH 7.8)的最小体积中再溶解。在上清液中加入固体(NH4)2SO4，使其达到70%的饱和度。1小时后，收集第二次沉淀，在0.1 M KCl, 5 mm k -磷酸盐和10 /LM EDTA (pH 7.8)中重悬并透析。通过凝胶排斥层析进一步纯化酶。首先将其应用于用透析缓冲液平衡的Sephadex G-100柱(2 x 90 cm)上。柱的空隙体积为74.5 ml，流速为0.2 ml/min。该柱用已知mol wt(9)的蛋白质进行校准。比活性大于300单位/毫克蛋白质的馏分从70%饱和(NH，)2SO溶液中混合并盐化。沉淀物经离心收集，溶解于小体积的蒸馏水中，在洗脱缓冲液中透析。然后将其涂在用相同缓冲液平衡的Bio-Gel P-30柱(1 x 60 cm)上。该色谱柱除去了一些较高摩尔重量的杂质。将比活性超过700单位/mg的馏分按上述方法合并浓缩。酶在相同的BioGel P-30柱上重新层析。摩尔重量稍低的杂质部分从酶中分离出来。这次只有最大比活性的两个部分(约2000单位/毫克)被合并。用冷冻丙酮分馏除去额外的杂质。在1.5 ~ 2体积的丙酮之间得到了最有效的馏分。最后一馏分的沉淀物在0.05 M k -磷酸盐(pH 7.8)中再溶解。
{"title":"Superoxide Dismutases","authors":"W. Van Camp, M. Van Montagu, D. Inzé","doi":"10.1201/9781351070454-12","DOIUrl":"https://doi.org/10.1201/9781351070454-12","url":null,"abstract":"Superoxide dismutase was purified from pea (Pisum sativum L., cv. Wando) seeds and corn (Zea mays L., cv. Michigan 500) seedlings. The purified pea enzyme eluting as a single peak from gel exclusion chromatography columns contained the three electrophoreticaUy distinct bands of superoxide dismutase characterizing the crude extract. The purified corn enzyme eluted as the same peak as the pea enzyme, and contained five of the seven active bands found in the crude extract. The similar molecular weights and the cyanide sensitivities of these bands indicated that they are probably isozymes of a cupro-zinc superoxide dismutase. One of the remaining corn bands was shown to be a peroxidase. Superoxide dismutase accounted for 1.6 to 2.4% of the water-soluble protein in seedlings of corn, peas, and oats (Avena sativa L., cv. Au Sable). The superoxide dismutase activity per plant and per milligram water-soluble protein considerably increased during germination of oats and during greening and hook opening of peas. In a previous study, considerable amounts of SOD3 were found to be present in roots, shoots, seeds, and seed parts of oats, corn, and peas (4). Electrophoresis indicated multiple forms of the enzyme. Significant differences in quantity and forms of the enzyme were observed between species and between organs within a species. The objective of this study was to substantiate further the occurrence of the enzyme in higher plants and to examine the observed differences between species. For this purpose the enzyme was purified. Changes of SOD activity during seedling growth were also studied. MATERIALS AND METHODS Enzyme Purification. Unless otherwise stated, all operations were performed at 0 to 4 C. Dry pea seeds (Pisum sativum L., cv. Wando) were soaked in distilled H20 for about 15 hr. The resulting 1650 g wet weight was crushed with an electric mortar and pestle and homogenized with 1 liter of 0.1 M K2HPO4 in a Waring Blendor. The resulting pH was 7.5. After stirring, the slurry was filtered/squeezed through six layers of cheesecloth. The filtrate was centrifuged twice at 13000g for 30 min in a Sorvall RC2-B refrigerated centrifuge. The supernatant was subjected to the Tsuchihashi (chloroform-ethanol) treatment essentially as described by Weisiger and I Michigan Agricultural Experiment Station Journal Article No. 7765. 2 This paper represents part of the Ph.D. dissertation of C. N. G. Abbreviations: SOD: superoxide dismutase (EC 1 .15.1.1); NBT: pnitro blue tetrazolium chloride. Fridovich (10). None of the pea SOD enzymes is inactivated by this treatment. The supernatant was mixed with 0.25 volume of ethanol and 0.15 volume of chloroform and stirred for 15 min. It was then clarified by centrifugation at 13000g for 15 min. Chloroform that was separated out during centrifugation was removed by suction. The supernatant was decanted, solid K2HPO4 (20 g/l) was added, and the two phases were separated after 30 min. The less dense, ethanol-rich phase was c","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91402675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Photooxidative Stress in Trees","authors":"A. Polle, H. Rennenberg","doi":"10.1201/9781351070454-8","DOIUrl":"https://doi.org/10.1201/9781351070454-8","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86979296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Production and Action of Active Oxygen Species in Photosynthetic Tissues","authors":"K. Asada, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-3","DOIUrl":"https://doi.org/10.1201/9781351070454-3","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76821133","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1201/9781351070454-14
K. Tanaka, C. Foyer, P. Mullineaux
{"title":"Tolerance to Herbicides and Air Pollutants","authors":"K. Tanaka, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-14","DOIUrl":"https://doi.org/10.1201/9781351070454-14","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73508222","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Role of Oxygen in Photoinhibition of Photosynthesis*","authors":"G. Krause, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-2","DOIUrl":"https://doi.org/10.1201/9781351070454-2","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89571981","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N. Doke, Y. Miura, L. M. Sanchez, K. Kawakita, C. Foyer, P. Mullineaux
{"title":"Involvement of Superoxide in Signal Transduction: Responses to Attack by Pathogens, Physical and Chemical Shocks, and UV Irradiation","authors":"N. Doke, Y. Miura, L. M. Sanchez, K. Kawakita, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-7","DOIUrl":"https://doi.org/10.1201/9781351070454-7","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75744814","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1201/9781351070454-10
J. Gressel, E. Galun, C. Foyer, P. Mullineaux
{"title":"Genetic Controls of Photooxidant Tolerance","authors":"J. Gressel, E. Galun, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-10","DOIUrl":"https://doi.org/10.1201/9781351070454-10","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86973119","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Chilling Stress and Photosynthesis","authors":"N. Baker, C. Foyer, P. Mullineaux","doi":"10.1201/9781351070454-5","DOIUrl":"https://doi.org/10.1201/9781351070454-5","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84787318","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-01-01DOI: 10.1201/9781351070454-11
J. G. Scandalios
{"title":"Regulation and Properties of Plant Catalases","authors":"J. G. Scandalios","doi":"10.1201/9781351070454-11","DOIUrl":"https://doi.org/10.1201/9781351070454-11","url":null,"abstract":"","PeriodicalId":9661,"journal":{"name":"Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91152146","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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