{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T18:30:02Z","timestamp":1761762602579},"reference-count":0,"publisher":"Rockefeller University Press","issue":"2","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1986,8,1]]},"abstract":"<jats:p>Two Triton-insoluble fractions were isolated from Acanthamoeba castellanii. The major non-membrane proteins in both fractions were actin (30-40%), myosin II (4-9%), myosin I (1-5%), and a 55-kD polypeptide (10%). The 55-kD polypeptide did not react with antibodies against tubulins from turkey brain, paramecium, or yeast. All of these proteins were much more concentrated in the Triton-insoluble fractions than in the whole homogenate or soluble supernatant. The 55-kD polypeptide was extracted with 0.3 M NaCl, fractionated by ammonium sulfate, and purified to near homogeneity by DEAE-cellulose and hydroxyapatite chromatography. The purified protein had a molecular mass of 110 kD and appeared to be a homodimer by isoelectric focusing. The 110-kD dimer bound to F-actin with a maximal binding stoichiometry of 0.5 mol\/mol of actin (1 mol of 55-kD subunit\/mol of actin). Although the 110-kD protein enhanced the sedimentation of F-actin, it did not affect the low shear viscosity of F-actin solutions nor was bundling of F-actin observed by electron microscopy. The 110-kD dimer protein inhibited the actin-activated Mg2+-ATPase activities of Acanthamoeba myosin I and myosin II in a concentration-dependent manner. By indirect immunofluorescence, the 110-kD protein was found to be localized in the peripheral cytoplasm near the plasma membrane which is also enriched in F-actin filaments and myosin I.<\/jats:p>","DOI":"10.1083\/jcb.103.2.621","type":"journal-article","created":{"date-parts":[[2004,5,15]],"date-time":"2004-05-15T00:18:20Z","timestamp":1084580300000},"page":"621-630","update-policy":"http:\/\/dx.doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":4,"title":["Isolation and partial characterization of a 110-kD dimer actin-binding protein."],"prefix":"10.1083","volume":"103","author":[{"given":"T","family":"Ueno","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E D","family":"Korn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1986,8,1]]},"container-title":["The Journal of cell biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/103\/2\/621\/1459309\/621.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/103\/2\/621\/1459309\/621.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,21]],"date-time":"2023-07-21T23:29:20Z","timestamp":1689982160000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/103\/2\/621\/55229\/Isolation-and-partial-characterization-of-a-110-kD"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1986,8,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1986,8,1]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.103.2.621","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1986,8,1]]}}}