{"title":"蟋蟀早期卵疟原虫肌动蛋白样蛋白的纯化及部分特性研究。","authors":"J G Moser","doi":"10.1007/BF00575324","DOIUrl":null,"url":null,"abstract":"<p><p>The purification of an actin-like protein from cricket egg yolk plasmodia by different selective extraction procedures, ammonium sulphate precipitation, ion exchange and immunoabsorption chromatography is described. Criteria of purity from analytical ultracentrifugation, SDS-disc electrophoresis, and immunoelectrophoresis are presented. Immunodiffusion analysis was used to control the success of the purification procedures.The molecular weight of the monomeric form is 60000±10%. Polymerization to pearl-chain aggregate structures occurs under different conditions in 0.1 M KCl in the presence of ATP. Vinblastine precipitation leads to similar structures. Possibly related structures and the possible rÔle of this protein in organizing movements in the plasmodial system are discussed.</p>","PeriodicalId":54406,"journal":{"name":"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen","volume":"176 4","pages":"329-346"},"PeriodicalIF":0.0000,"publicationDate":"1975-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF00575324","citationCount":"0","resultStr":"{\"title\":\"Purification and partial characterization of an actin-like protein from cricket early egg plasmodium.\",\"authors\":\"J G Moser\",\"doi\":\"10.1007/BF00575324\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The purification of an actin-like protein from cricket egg yolk plasmodia by different selective extraction procedures, ammonium sulphate precipitation, ion exchange and immunoabsorption chromatography is described. Criteria of purity from analytical ultracentrifugation, SDS-disc electrophoresis, and immunoelectrophoresis are presented. Immunodiffusion analysis was used to control the success of the purification procedures.The molecular weight of the monomeric form is 60000±10%. Polymerization to pearl-chain aggregate structures occurs under different conditions in 0.1 M KCl in the presence of ATP. Vinblastine precipitation leads to similar structures. Possibly related structures and the possible rÔle of this protein in organizing movements in the plasmodial system are discussed.</p>\",\"PeriodicalId\":54406,\"journal\":{\"name\":\"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen\",\"volume\":\"176 4\",\"pages\":\"329-346\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1975-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/BF00575324\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/BF00575324\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Wilhelm Roux Archiv Fur Entwicklungsmechanik Der Organismen","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF00575324","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
采用不同的选择性提取、硫酸铵沉淀、离子交换和免疫吸收层析等方法从蟋蟀卵黄疟原虫中纯化一种肌动蛋白样蛋白。给出了分析性超离心、sds -圆盘电泳和免疫电泳的纯度标准。免疫扩散分析用于控制纯化过程的成功。单体形式的分子量为60000±10%。在0.1 M KCl中，在ATP的存在下，在不同条件下聚合成珍珠链聚集体结构。长春碱沉淀导致类似的结构。讨论了可能的相关结构和该蛋白在组织浆体系统运动中的可能rÔle。
Purification and partial characterization of an actin-like protein from cricket early egg plasmodium.
The purification of an actin-like protein from cricket egg yolk plasmodia by different selective extraction procedures, ammonium sulphate precipitation, ion exchange and immunoabsorption chromatography is described. Criteria of purity from analytical ultracentrifugation, SDS-disc electrophoresis, and immunoelectrophoresis are presented. Immunodiffusion analysis was used to control the success of the purification procedures.The molecular weight of the monomeric form is 60000±10%. Polymerization to pearl-chain aggregate structures occurs under different conditions in 0.1 M KCl in the presence of ATP. Vinblastine precipitation leads to similar structures. Possibly related structures and the possible rÔle of this protein in organizing movements in the plasmodial system are discussed.
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