Purification and properties of normal human α 1-antitrypsin
Identifieur interne : 003D46 ( Istex/Corpus ); précédent : 003D45; suivant : 003D47Purification and properties of normal human α 1-antitrypsin
Auteurs : Irving P. CrawfordSource :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1973.
Abstract
A relatively gentle purification method has been devised for the major serine-protease inhibitor in human plasma. The product, a single chain glycoprotein of 50,000 molecular weight, is obtained in 25% yield. It contains 11.5% carbohydrate by weight, a single residue of cysteine and two of tryptophan. N-terminal glutamate or glutamine was found by dansylation. Isoelectric focusing at high resolution in acrylamide gels revealed three major and several minor protein species. Several possible mechanisms to account for this isoelectric microheterogeneity are discussed.
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DOI: 10.1016/0003-9861(73)90359-7
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The product, a single chain glycoprotein of 50,000 molecular weight, is obtained in 25% yield. It contains 11.5% carbohydrate by weight, a single residue of cysteine and two of tryptophan. N-terminal glutamate or glutamine was found by dansylation. Isoelectric focusing at high resolution in acrylamide gels revealed three major and several minor protein species. Several possible mechanisms to account for this isoelectric microheterogeneity are discussed.</p></abstract><textClass><keywords scheme="keyword"><list><head>Article category</head><item><term>Immunochemistry</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1973-01-12">Received</change><change when="1973">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YABBI</jid><aid>73903597</aid><ce:pii>0003-9861(73)90359-7</ce:pii><ce:doi>10.1016/0003-9861(73)90359-7</ce:doi><ce:copyright type="unknown" year="1973"></ce:copyright><ce:doctopics><ce:doctopic><ce:text>Immunochemistry</ce:text></ce:doctopic></ce:doctopics></item-info><head><ce:title>Purification and properties of normal human <ce:italic>α</ce:italic><ce:inf loc="post">1</ce:inf>-antitrypsin</ce:title><ce:author-group><ce:author><ce:given-name>Irving P.</ce:given-name><ce:surname>Crawford</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92037 U.S.A.</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="12" month="1" year="1973"></ce:date-received><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">A relatively gentle purification method has been devised for the major serine-protease inhibitor in human plasma. The product, a single chain glycoprotein of 50,000 molecular weight, is obtained in 25% yield. It contains 11.5% carbohydrate by weight, a single residue of cysteine and two of tryptophan. N-terminal glutamate or glutamine was found by dansylation. Isoelectric focusing at high resolution in acrylamide gels revealed three major and several minor protein species. Several possible mechanisms to account for this isoelectric microheterogeneity are discussed.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Purification and properties of normal human α 1-antitrypsin</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Purification and properties of normal human</title></titleInfo><name type="personal"><namePart type="given">Irving P.</namePart><namePart type="family">Crawford</namePart><affiliation>Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92037 U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1973</dateIssued><dateCaptured encoding="w3cdtf">1973-01-12</dateCaptured><copyrightDate encoding="w3cdtf">1973</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">A relatively gentle purification method has been devised for the major serine-protease inhibitor in human plasma. 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