{"title":"Lipoprotein-X。","authors":"S Narayanan","doi":"10.3109/10408367909105853","DOIUrl":null,"url":null,"abstract":"<p><p>Lipoprotein-X is an abnormal lipoprotein that appears in the sera of patients with obstructive jaundice, and thus is a sensitive indicator of cholestasis. In patients with familial plasma lecithin, Cholesterol acyltransferase (LCAT) deficiency, there is an inverse relationship between plasma Lp-X levels and LCAT activity. Ultracentrifugation procedures utilized for isolation of Lp-X have shown that it is associated with the low density lipoprotein fraction. Lp-X can be visualized by electrophoresis on either Agar or Agarose. The purity of Lp-X preparations has been documented by immunochemical procedures. The availability of highly purified antisera to Lp-X has served as a basis of one of the assay procedures for this lipoprotein. It's chemical composition has been established. Phospholipids and unesterified cholesterol constitute the bulk of the Lp-X molecule. Electron microscopic studies have demonstrated that Lp-X is a spherical particle which has strong aggregating properties. Membrane bound enzymes have been shown to aggregate with Lp-X. The fact that bile lipoprotein can be converted to Lp-X by the addition of albumin and that Lp-X can be converted to bile lipoprotein by the addition of bile salts offers a possible explanation for the origins of Lp-X. Phospholipases of plasma might play a role in the catabolism of Lp-X. The value and limitations of Lp-X determinations will also be addressed in this review.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"11 1","pages":"31-51"},"PeriodicalIF":0.0000,"publicationDate":"1979-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909105853","citationCount":"0","resultStr":"{\"title\":\"Lipoprotein-X.\",\"authors\":\"S Narayanan\",\"doi\":\"10.3109/10408367909105853\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Lipoprotein-X is an abnormal lipoprotein that appears in the sera of patients with obstructive jaundice, and thus is a sensitive indicator of cholestasis. In patients with familial plasma lecithin, Cholesterol acyltransferase (LCAT) deficiency, there is an inverse relationship between plasma Lp-X levels and LCAT activity. Ultracentrifugation procedures utilized for isolation of Lp-X have shown that it is associated with the low density lipoprotein fraction. Lp-X can be visualized by electrophoresis on either Agar or Agarose. The purity of Lp-X preparations has been documented by immunochemical procedures. The availability of highly purified antisera to Lp-X has served as a basis of one of the assay procedures for this lipoprotein. It's chemical composition has been established. Phospholipids and unesterified cholesterol constitute the bulk of the Lp-X molecule. Electron microscopic studies have demonstrated that Lp-X is a spherical particle which has strong aggregating properties. Membrane bound enzymes have been shown to aggregate with Lp-X. The fact that bile lipoprotein can be converted to Lp-X by the addition of albumin and that Lp-X can be converted to bile lipoprotein by the addition of bile salts offers a possible explanation for the origins of Lp-X. Phospholipases of plasma might play a role in the catabolism of Lp-X. The value and limitations of Lp-X determinations will also be addressed in this review.</p>\",\"PeriodicalId\":75746,\"journal\":{\"name\":\"CRC critical reviews in clinical laboratory sciences\",\"volume\":\"11 1\",\"pages\":\"31-51\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.3109/10408367909105853\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"CRC critical reviews in clinical laboratory sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/10408367909105853\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"CRC critical reviews in clinical laboratory sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10408367909105853","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Lipoprotein-X is an abnormal lipoprotein that appears in the sera of patients with obstructive jaundice, and thus is a sensitive indicator of cholestasis. In patients with familial plasma lecithin, Cholesterol acyltransferase (LCAT) deficiency, there is an inverse relationship between plasma Lp-X levels and LCAT activity. Ultracentrifugation procedures utilized for isolation of Lp-X have shown that it is associated with the low density lipoprotein fraction. Lp-X can be visualized by electrophoresis on either Agar or Agarose. The purity of Lp-X preparations has been documented by immunochemical procedures. The availability of highly purified antisera to Lp-X has served as a basis of one of the assay procedures for this lipoprotein. It's chemical composition has been established. Phospholipids and unesterified cholesterol constitute the bulk of the Lp-X molecule. Electron microscopic studies have demonstrated that Lp-X is a spherical particle which has strong aggregating properties. Membrane bound enzymes have been shown to aggregate with Lp-X. The fact that bile lipoprotein can be converted to Lp-X by the addition of albumin and that Lp-X can be converted to bile lipoprotein by the addition of bile salts offers a possible explanation for the origins of Lp-X. Phospholipases of plasma might play a role in the catabolism of Lp-X. The value and limitations of Lp-X determinations will also be addressed in this review.