{"title":"Ontogeny and tissue distribution of alpha-1-antitrypsin of the mouse","authors":"Louis Lamontagne , Jack Gauldie , Alex Koj","doi":"10.1016/0005-2744(81)90217-5","DOIUrl":null,"url":null,"abstract":"<div><p><span><math><mtext>α</mtext><msub><mi></mi><mn>1</mn></msub><mtext>-</mtext><mtext>Antitrypsin</mtext></math></span> is the second most abundant proteinase inhibitor in plasma. The fact that it is a globular glycoprotein of relatively small size (<span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub></math></span> 53 500) allows it access to a wide variety of fluids and tissue sites. <span><math><mtext>α</mtext><msub><mi></mi><mn>1</mn></msub><mtext>-</mtext><mtext>Antitrypsin</mtext></math></span> has been purified from mouse plasma by affinity chromatography and ion exchange. The purified protein exhibits homogeneity on polyacrylamide electrophoresis, but electrophoretic heterogeneity on crossed immuno-electrophoresis. Mouse and rat <span><math><mtext>α</mtext><msub><mi></mi><mn>1</mn></msub><mtext>-</mtext><mtext>antitrypsin</mtext></math></span> show strong crossreactivity and the half-life for mouse <span><math><mtext>α</mtext><msub><mi></mi><mn>1</mn></msub><mtext>-</mtext><mtext>antitrypsin</mtext></math></span> is 15.5 h. Fetal levels are 15% of adult and it requires 25–30 days before adult levels are reached in the neonate. Maternal levels remain unchanged throughout pregnancy and at parturition. The inhibitor is present in a number of body fluids including serum, breast milk, gastrointestinal washings, lung washings and bile. The source of <span><math><mtext>α</mtext><msub><mi></mi><mn>1</mn></msub><mtext>-</mtext><mtext>antitrypsin</mtext></math></span> for all of these fluids appears to be the liver.</p></div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":"662 1","pages":"Pages 15-21"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90217-5","citationCount":"11","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005274481902175","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 11
Abstract
is the second most abundant proteinase inhibitor in plasma. The fact that it is a globular glycoprotein of relatively small size ( 53 500) allows it access to a wide variety of fluids and tissue sites. has been purified from mouse plasma by affinity chromatography and ion exchange. The purified protein exhibits homogeneity on polyacrylamide electrophoresis, but electrophoretic heterogeneity on crossed immuno-electrophoresis. Mouse and rat show strong crossreactivity and the half-life for mouse is 15.5 h. Fetal levels are 15% of adult and it requires 25–30 days before adult levels are reached in the neonate. Maternal levels remain unchanged throughout pregnancy and at parturition. The inhibitor is present in a number of body fluids including serum, breast milk, gastrointestinal washings, lung washings and bile. The source of for all of these fluids appears to be the liver.