{"title":"热处理对水藻CH3氢化酶的部分纯化。","authors":"S H Wang, P C Chen","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The methylviologen-dependent hydrogenase of Anabaena sp. CH3 is unstable at 4 degrees C and in air. All the purifying procedures were carried out at 25 degrees C and under argon atmosphere. The enzyme was partially purified by the following steps: heat treatment, DEAE-cellulose ion-exchange chromatography and gel filtration on TSK-Fractogel. Experimental results indicated that the heat-treatment procedure was beneficial for the separation of the enzyme from phycobiliproteins.</p>","PeriodicalId":24009,"journal":{"name":"Zhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Partial purification of hydrogenase from Anabaena sp. CH3 with heat treatment.\",\"authors\":\"S H Wang, P C Chen\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The methylviologen-dependent hydrogenase of Anabaena sp. CH3 is unstable at 4 degrees C and in air. All the purifying procedures were carried out at 25 degrees C and under argon atmosphere. The enzyme was partially purified by the following steps: heat treatment, DEAE-cellulose ion-exchange chromatography and gel filtration on TSK-Fractogel. Experimental results indicated that the heat-treatment procedure was beneficial for the separation of the enzyme from phycobiliproteins.</p>\",\"PeriodicalId\":24009,\"journal\":{\"name\":\"Zhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Partial purification of hydrogenase from Anabaena sp. CH3 with heat treatment.
The methylviologen-dependent hydrogenase of Anabaena sp. CH3 is unstable at 4 degrees C and in air. All the purifying procedures were carried out at 25 degrees C and under argon atmosphere. The enzyme was partially purified by the following steps: heat treatment, DEAE-cellulose ion-exchange chromatography and gel filtration on TSK-Fractogel. Experimental results indicated that the heat-treatment procedure was beneficial for the separation of the enzyme from phycobiliproteins.
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