{"title":"β-肌动蛋白对f -肌动蛋白颗粒长度的影响","authors":"K. Maruyama","doi":"10.1016/0926-6585(66)90076-8","DOIUrl":null,"url":null,"abstract":"<div><p>The binding of β-actinin, the actin-dispersing factor, to F-actin has been investigated. The stoichiometric ratios for the binding of β-actinin to F-actin were found to be 1:10 and 1:8, by weight, for intact and sonicated F-actin, respectively.</p><p>When an increasing amount of β-actinin was added to F-actin and subjected to sonication, F-actin could be dispersed into particles as short as 3000–4000 Å. Such short F-actin particles were also formed when G-actin was polymerized in the presence of a large amount of β-actinin.</p><p>Experimental conditions were checked for the action of β-actinin on the apparent particle length of F-actin. β-Actinin was found to become slowly inactivated in 0.1 M KCl.</p></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"126 2","pages":"Pages 389-398"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90076-8","citationCount":"19","resultStr":"{\"title\":\"Effect of β-actinin on the particle length of F-actin\",\"authors\":\"K. Maruyama\",\"doi\":\"10.1016/0926-6585(66)90076-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The binding of β-actinin, the actin-dispersing factor, to F-actin has been investigated. The stoichiometric ratios for the binding of β-actinin to F-actin were found to be 1:10 and 1:8, by weight, for intact and sonicated F-actin, respectively.</p><p>When an increasing amount of β-actinin was added to F-actin and subjected to sonication, F-actin could be dispersed into particles as short as 3000–4000 Å. Such short F-actin particles were also formed when G-actin was polymerized in the presence of a large amount of β-actinin.</p><p>Experimental conditions were checked for the action of β-actinin on the apparent particle length of F-actin. β-Actinin was found to become slowly inactivated in 0.1 M KCl.</p></div>\",\"PeriodicalId\":100158,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis\",\"volume\":\"126 2\",\"pages\":\"Pages 389-398\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6585(66)90076-8\",\"citationCount\":\"19\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926658566900768\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926658566900768","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Effect of β-actinin on the particle length of F-actin
The binding of β-actinin, the actin-dispersing factor, to F-actin has been investigated. The stoichiometric ratios for the binding of β-actinin to F-actin were found to be 1:10 and 1:8, by weight, for intact and sonicated F-actin, respectively.
When an increasing amount of β-actinin was added to F-actin and subjected to sonication, F-actin could be dispersed into particles as short as 3000–4000 Å. Such short F-actin particles were also formed when G-actin was polymerized in the presence of a large amount of β-actinin.
Experimental conditions were checked for the action of β-actinin on the apparent particle length of F-actin. β-Actinin was found to become slowly inactivated in 0.1 M KCl.