P. Becuwe , J. van Beeumen , B. Samyn , J.P. Touzel , C. Slomianny , D. Camus , D. Dive
{"title":"巴贝斯虫超氧化物歧化酶的纯化、鉴定及氨基末端序列分析","authors":"P. Becuwe , J. van Beeumen , B. Samyn , J.P. Touzel , C. Slomianny , D. Camus , D. Dive","doi":"10.1016/0305-0491(94)90126-0","DOIUrl":null,"url":null,"abstract":"<div><p><em>Babesia hylomysci</em> was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (p<em>I</em>) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this <em>N</em>-terminal sequence of <em>B. hylomysci</em> SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 637-645"},"PeriodicalIF":0.0000,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90126-0","citationCount":"5","resultStr":"{\"title\":\"Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci\",\"authors\":\"P. Becuwe , J. van Beeumen , B. Samyn , J.P. Touzel , C. Slomianny , D. Camus , D. Dive\",\"doi\":\"10.1016/0305-0491(94)90126-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><em>Babesia hylomysci</em> was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (p<em>I</em>) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this <em>N</em>-terminal sequence of <em>B. hylomysci</em> SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.</p></div>\",\"PeriodicalId\":100294,\"journal\":{\"name\":\"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry\",\"volume\":\"109 4\",\"pages\":\"Pages 637-645\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0305-0491(94)90126-0\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0305049194901260\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0305049194901260","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci
Babesia hylomysci was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (pI) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this N-terminal sequence of B. hylomysci SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.
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