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Article: A rat serum glycoprotein whose synthesis rate increases greatly during inflammation

TitleA rat serum glycoprotein whose synthesis rate increases greatly during inflammation
Authors
Issue Date1979
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1979, v. 254 n. 21, p. 10565-10568 How to Cite?
AbstractCrossed immunoelectrophoresis of rat serum demonstrated considerably increased serum concentrations of at least ten different proteins during turpentine-induced inflammation. One protein, which moved during electrophoresis like an α1 globulin, showed a particularly large increase. This protein was purified to homogeneity by ammmonium sulfate fractionation followed by chromatography on DEAE-cellulose, Sephadex G-100, and concanavalin A-Sepharose, and finally disc electrophoresis in polyacrylamide gel. It has a molecular weight of 56,000 determined by equilibrium ultracentrifugation. An apparent molecular weight of 68,000 was estimated for the reduced protein by electrophoresis in polyacrylamide gel plus sodium dodecyl sulfate, suggesting that the native protein is composed of a single polypeptide chain. It has an E(1%)(280, 1cm) of 5.2, an isoelectric pH of 4.7 and contains 19% carbohydrate. The protein does not inhibit bovine trypsin or chymotrypsin. Its physical properties and amino acid composition distinguish this protein from all other rat serum proteins hitherto characterized. During acute inflammation, induced 25 h previously, rats incorporated 20 times more [14C]leucine into this particular protein than did normal rats. However, incorporation into total serum protein during acute inflammation increased only slightly. Regardless of whether inflammation was induced by surgical injury or by a subcutaneous turpentine injection, within 48 h the serum concentration of this major acute-phase protein rose from the normal value of 0.46 g/liter to a maximum value of 7.2 g/liter, which constituted 10% of the total serum protein.
Persistent Identifierhttp://hdl.handle.net/10722/147299
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorUrban, Jen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorSchreiber, Gen_US
dc.date.accessioned2012-05-29T06:02:46Z-
dc.date.available2012-05-29T06:02:46Z-
dc.date.issued1979en_US
dc.identifier.citationJournal Of Biological Chemistry, 1979, v. 254 n. 21, p. 10565-10568en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147299-
dc.description.abstractCrossed immunoelectrophoresis of rat serum demonstrated considerably increased serum concentrations of at least ten different proteins during turpentine-induced inflammation. One protein, which moved during electrophoresis like an α1 globulin, showed a particularly large increase. This protein was purified to homogeneity by ammmonium sulfate fractionation followed by chromatography on DEAE-cellulose, Sephadex G-100, and concanavalin A-Sepharose, and finally disc electrophoresis in polyacrylamide gel. It has a molecular weight of 56,000 determined by equilibrium ultracentrifugation. An apparent molecular weight of 68,000 was estimated for the reduced protein by electrophoresis in polyacrylamide gel plus sodium dodecyl sulfate, suggesting that the native protein is composed of a single polypeptide chain. It has an E(1%)(280, 1cm) of 5.2, an isoelectric pH of 4.7 and contains 19% carbohydrate. The protein does not inhibit bovine trypsin or chymotrypsin. Its physical properties and amino acid composition distinguish this protein from all other rat serum proteins hitherto characterized. During acute inflammation, induced 25 h previously, rats incorporated 20 times more [14C]leucine into this particular protein than did normal rats. However, incorporation into total serum protein during acute inflammation increased only slightly. Regardless of whether inflammation was induced by surgical injury or by a subcutaneous turpentine injection, within 48 h the serum concentration of this major acute-phase protein rose from the normal value of 0.46 g/liter to a maximum value of 7.2 g/liter, which constituted 10% of the total serum protein.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAlpha-Globulins - Analysis - Biosynthesisen_US
dc.subject.meshAmino Acids - Analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarbohydrates - Analysisen_US
dc.subject.meshGlycoproteins - Biosynthesis - Blooden_US
dc.subject.meshImmunoelectrophoresis, Two-Dimensionalen_US
dc.subject.meshInflammation - Blood - Chemically Induceden_US
dc.subject.meshLiver Neoplasms, Experimental - Blooden_US
dc.subject.meshMaleen_US
dc.subject.meshRatsen_US
dc.subject.meshTurpentineen_US
dc.titleA rat serum glycoprotein whose synthesis rate increases greatly during inflammationen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid91605en_US
dc.identifier.scopuseid_2-s2.0-0018604129en_US
dc.identifier.volume254en_US
dc.identifier.issue21en_US
dc.identifier.spage10565en_US
dc.identifier.epage10568en_US
dc.identifier.isiWOS:A1979HU44900001-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridUrban, J=7202366494en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridSchreiber, G=7202599943en_US

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