{"title":"糖酵解酶与细胞骨架的关联。","authors":"H R Knull, J L Walsh","doi":"10.1016/b978-0-12-152833-1.50007-1","DOIUrl":null,"url":null,"abstract":"<p><p>The diverse physical associations of the glycolytic enzymes with structural components of the cell suggest that the glycolytic enzymes are not entirely soluble in the cell. The relatively low affinities of the associations are likely responsible for the apparently transient interactions. The binding phenomenon is suggested to regulate metabolism through changes in enzymatic activity and facilitates localized enrichment of the enzymes.</p>","PeriodicalId":10933,"journal":{"name":"Current topics in cellular regulation","volume":"33 ","pages":"15-30"},"PeriodicalIF":0.0000,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/b978-0-12-152833-1.50007-1","citationCount":"132","resultStr":"{\"title\":\"Association of glycolytic enzymes with the cytoskeleton.\",\"authors\":\"H R Knull, J L Walsh\",\"doi\":\"10.1016/b978-0-12-152833-1.50007-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The diverse physical associations of the glycolytic enzymes with structural components of the cell suggest that the glycolytic enzymes are not entirely soluble in the cell. The relatively low affinities of the associations are likely responsible for the apparently transient interactions. The binding phenomenon is suggested to regulate metabolism through changes in enzymatic activity and facilitates localized enrichment of the enzymes.</p>\",\"PeriodicalId\":10933,\"journal\":{\"name\":\"Current topics in cellular regulation\",\"volume\":\"33 \",\"pages\":\"15-30\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/b978-0-12-152833-1.50007-1\",\"citationCount\":\"132\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current topics in cellular regulation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/b978-0-12-152833-1.50007-1\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current topics in cellular regulation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/b978-0-12-152833-1.50007-1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Association of glycolytic enzymes with the cytoskeleton.
The diverse physical associations of the glycolytic enzymes with structural components of the cell suggest that the glycolytic enzymes are not entirely soluble in the cell. The relatively low affinities of the associations are likely responsible for the apparently transient interactions. The binding phenomenon is suggested to regulate metabolism through changes in enzymatic activity and facilitates localized enrichment of the enzymes.
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