ArticleJournal of muscle research and cell motility1989
Isolation and characterization of gelsolin from cultured BHK cells.
Article in Journal of muscle research and cell motility, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 2 citations in OpenAlex.
- Gel electrophoresis of native gelsolin and gelsolin-actin complexes.Journal of muscle research and cell motility · 1990Article
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1 author at 1 institution in 1 country.
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Abstract
The Ca2+-dependent actin-polymerization nucleating protein of the cytoplasmic fraction of Baby hamster kidney (BHK) C13 cells has been isolated by anion-exchange, hydroxyapatite and gel-filtration chromatography. This protein has been identified as a cytoplasmic gelsolin by the following criteria: molecular mass of 90 kDa on SDS-PAGE, immunocrossreactivity with pig plasma gelsolin and similar actin-binding properties to gelsolins purified from other sources. BHK gelsolin forms a 1:2 ternary complex with rabbit muscle actin that is dependent on the presence of Ca2+. The ternary complex is dissociated on chelation of Ca2+ with EGTA to a binary complex and free actin. BHK gelsolin nucleates the polymerization of pyrene-labelled G-actin in a Ca2+-dependent manner. The proportion of unpolymerized monomer is increased in the presence of BHK gelsolin by an amount consistent with capping of the positive filament ends. The rate of actin depolymerization induced by diluting F-actin to below its critical concentration (Cc) is unaffected by the presence of BHK gelsolin in EGTA. However, in the presence of Ca2+ the rate of depolymerization is increased indicating that BHK gelsolin severs actin filaments in a Ca2+-dependent manner.
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