Manfred P. Dierich , Beate Landen, Manfred Schmitt
{"title":"人血清中补体受体类似因子:1 .一种补体依赖性玫瑰花形成抑制分子的分离、α1-抗胰蛋白酶鉴定及其功能表征","authors":"Manfred P. Dierich , Beate Landen, Manfred Schmitt","doi":"10.1016/S0340-904X(79)80071-8","DOIUrl":null,"url":null,"abstract":"<div><p>A glycoprotein was isolated from human plasma which partially inhibited C3 carrying erythrocytes from binding to complement receptor cells (CR<sup>+</sup>C). Based on its physicochemical characteristics and its antigenicity this glycoprotein was identified as aI-antitrypsin (α<sub>1</sub>-AT). The activity of α<sub>1</sub>-AT towards-C3 and its fragments was unaffected by heating but it was destroyed by periodic acid. The isolated carbohydrate moiety of α<sub>1</sub>-AT showed the same effect as the intact molecule. Using F(ab)<sub>2</sub> of IgG-anti-α<sub>1</sub>-AT, α<sub>1</sub>-AT could be demonstrated on Raji cells and human erythrocytes. Treatment of these CR<sup>+</sup>C with IgG-anti-α<sub>1</sub>-AT resulted in a blockade of their C3 receptor activity. The results suggest, that α<sub>1</sub>-AT interacts through its carbohydrate portion with C3 and its fragments and functions as a complement receptor molecule.</p></div>","PeriodicalId":101288,"journal":{"name":"Zeitschrift für Immunit?tsforschung: Immunobiology","volume":"156 1","pages":"Pages 153-167"},"PeriodicalIF":0.0000,"publicationDate":"1979-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0340-904X(79)80071-8","citationCount":"8","resultStr":"{\"title\":\"Complement Receptor Analogous Factors in Human Serum: I. Isolation of a Molecule Inhibitory for Complement Dependent Rosette Formation, its Identification as α1-Antitrypsin and its Functional Characterization\",\"authors\":\"Manfred P. Dierich , Beate Landen, Manfred Schmitt\",\"doi\":\"10.1016/S0340-904X(79)80071-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A glycoprotein was isolated from human plasma which partially inhibited C3 carrying erythrocytes from binding to complement receptor cells (CR<sup>+</sup>C). Based on its physicochemical characteristics and its antigenicity this glycoprotein was identified as aI-antitrypsin (α<sub>1</sub>-AT). The activity of α<sub>1</sub>-AT towards-C3 and its fragments was unaffected by heating but it was destroyed by periodic acid. The isolated carbohydrate moiety of α<sub>1</sub>-AT showed the same effect as the intact molecule. Using F(ab)<sub>2</sub> of IgG-anti-α<sub>1</sub>-AT, α<sub>1</sub>-AT could be demonstrated on Raji cells and human erythrocytes. Treatment of these CR<sup>+</sup>C with IgG-anti-α<sub>1</sub>-AT resulted in a blockade of their C3 receptor activity. The results suggest, that α<sub>1</sub>-AT interacts through its carbohydrate portion with C3 and its fragments and functions as a complement receptor molecule.</p></div>\",\"PeriodicalId\":101288,\"journal\":{\"name\":\"Zeitschrift für Immunit?tsforschung: Immunobiology\",\"volume\":\"156 1\",\"pages\":\"Pages 153-167\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0340-904X(79)80071-8\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift für Immunit?tsforschung: Immunobiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0340904X79800718\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift für Immunit?tsforschung: Immunobiology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0340904X79800718","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Complement Receptor Analogous Factors in Human Serum: I. Isolation of a Molecule Inhibitory for Complement Dependent Rosette Formation, its Identification as α1-Antitrypsin and its Functional Characterization
A glycoprotein was isolated from human plasma which partially inhibited C3 carrying erythrocytes from binding to complement receptor cells (CR+C). Based on its physicochemical characteristics and its antigenicity this glycoprotein was identified as aI-antitrypsin (α1-AT). The activity of α1-AT towards-C3 and its fragments was unaffected by heating but it was destroyed by periodic acid. The isolated carbohydrate moiety of α1-AT showed the same effect as the intact molecule. Using F(ab)2 of IgG-anti-α1-AT, α1-AT could be demonstrated on Raji cells and human erythrocytes. Treatment of these CR+C with IgG-anti-α1-AT resulted in a blockade of their C3 receptor activity. The results suggest, that α1-AT interacts through its carbohydrate portion with C3 and its fragments and functions as a complement receptor molecule.
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