{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,23]],"date-time":"2023-11-23T22:35:31Z","timestamp":1700778931824},"reference-count":22,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":11632,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1973,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The Rapidly Migrating Proteins (RMP) which shuttle nonrandomly between nucleus and cytoplasm and equilibrate in approximately equal amounts in each compartment, were isolated from <jats:italic>Amoeba proteus<\/jats:italic> by implanting <jats:sup>3<\/jats:sup>H\u2010protein containing nuclei into unlabeled cells and some time later extracting the labeled material from the cytoplasms of such cells. The labeled material was subsequently fractionated by gel filtration in Sephadex G\u2010100 columns. The RMP are soluble in dilute salt solutions and appear as a heterogenous group of molecules, one component of which seems to be a single species of protein accounting for ca. one\u2010third of the RMP fraction. Because of its distinctness this component, called the LR fraction, received the major attention in this study. LR was found to comprise ca. 17% of the aqueous\u2010soluble proteins of the nucleus and ca. 3\u20134% of the total cell protein.<\/jats:p><jats:p>LR has a very low molecular weight as determined, e.g., by its elution from a Sephadex G\u2010100 column. Because of its low molecular weight, LR could be purified by taking advantage of the fact that LR is (1) soluble in a saturated Solution of ammonium sulfate and (2) insoluble in butanol, diethyl ether, and 10% trichloroacetic acid.<\/jats:p><jats:p>LR migrates toward the anode as a single band when subjected to electrophoresis on \u201cstandard disc\u201d and SDS polyacrylamide gels. It does not enter a gel designed to separate basic proteins (at pH 4.0). When subjected to Sephadex G\u201025 gel filtration LR migrates through the gel as a single band and elutes from the gel at a position in the middle of the linear separation range that indicates its molecular weight is ca. 2300. The only N\u2010terminal amino acid found in the LR fraction is proline.<\/jats:p><jats:p>Evidence is presented to show that LR is not the product of a non\u2010specific breakdown of protein produced during its isolation, but the possibility that it results from the cleavage of a single chemical bond of a larger polypeptide, has not been eliminated.<\/jats:p><jats:p>When injected into non\u2010labeled amebae, purified radioactive LR concentrates in the nucleus \u2014 just as radioactive RMP concentrates in a recipient cell nucleus when an amino acid\u2010labeled nucleus is implanted into an unlabeled cell.<\/jats:p>","DOI":"10.1002\/jcp.1040810207","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T18:10:24Z","timestamp":1109441424000},"page":"181-197","source":"Crossref","is-referenced-by-count":19,"title":["Isolation and characterization of some of the proteins that shuttle between cytoplasm and nucleus in <i>Amoeba proteus<\/i>"],"prefix":"10.1002","volume":"81","author":[{"given":"Warren","family":"Jelinek","sequence":"first","affiliation":[]},{"given":"Lester","family":"Goldstein","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.48.1.202"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.40.3.622"},{"key":"e_1_2_1_4_1","first-page":"404","volume-title":"Gel Electrophoresis","author":"Davis B. 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