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The list of inhibitory proteins included platelet factor 4 (which has a cluster of lysine residues at its carboxyl terminus), two lysinerich histones, poly\u2010L\u2010lysines of chain length greater than 4, and protamine. These proteins were effective in the concentration range of 5\u201350 \u03bcg\/ml. Two other positively charged proteins, lysozyme and avidin, did not inhibit <jats:sup>125<\/jats:sup>I\u2010LDL binding. Kinetic studies suggested that protamine was not acting simply as a competitive inhibitor with regard to the LDL receptor. In light of previous data showing that polyanions such as heparin and polyphosphates also inhibit <jats:sup>125<\/jats:sup>I\u2010LDL binding to its cell surface receptor, the current findings suggest that charge interactions are important in this binding reaction. In a related series of studies, a number of glycoproteins and their asialo derivatives as well as a number of sugar phosphates failed to inhibit <jats:sup>125<\/jats:sup>I\u2010LDL binding to its receptor in fibroblasts.<\/jats:p>","DOI":"10.1002\/jss.400080302","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T05:25:29Z","timestamp":1117257929000},"page":"223-234","source":"Crossref","is-referenced-by-count":60,"title":["Inhibition of the binding of low\u2010density lipoprotein to its cell surface receptor in human fibroblasts by positively charged proteins"],"prefix":"10.1002","volume":"8","author":[{"given":"Michael S.","family":"Brown","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas F.","family":"Deuel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sandip K.","family":"Basu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph L.","family":"Goldstein","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2,19]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.174194"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-152811-9.50011-0"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.46.070177.004341"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(76)90258-0"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)45469-0"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.73.9.3178"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)66966-8"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)33600-1"},{"key":"e_1_2_1_10_2","unstructured":"MahleyRW InnerarityTL: In Kritchevsky D. 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