Effects of pH on the stability of the indium-113m blood protein complex and the selective binding of indium-113m to transferrin
Identifieur interne : 000595 ( Main/Exploration ); précédent : 000594; suivant : 000596Effects of pH on the stability of the indium-113m blood protein complex and the selective binding of indium-113m to transferrin
Auteurs : RBID : ISTEX:433_1987_Article_BF01851974.pdfEnglish descriptors
Abstract
Indium-113m (t1/2 = 100min; gamma-emission of 393keV) in trace amounts was injected i.v. in rats. Blood was collected by heart puncture 15 min after the injection, and blood plasma was separated by centrifugation. Gel filtration of plasma on Sephadex G-25M equilibrated with glycine/HCl (pH 2.2–3.6), NaHCO3/CO2 (pH 4.0–11.0) glycine/NaOH (pH 8.6–10.6) or sodium acetate/acetic acid (pH 3.0–5.0) was used to separate free indium from indium bound to macromolecular proteins. Determination of radioactivity in eluted fractions showed that more than 85% of the plasma indium was bound to macromolecules at pH values between 5.0 and pH 10.6. However, dissociation of the indium plasma protein complexes occurred at pH values below 5.5, and more than 90% of the indium radioactivity was found in the low molecular weight fraction at pH 2.2.Affinity chromatography using immobilized antibodies to rat transferrin was used to isolate transferrin at pH 7.4 and 5.5. Immunodiffusion and electrophoresis were used to identify the proteins in fractions obtained by affinity chromatography. It was found that the indium-113m activity was correlated with the content of transferrin and that 80%–90% of this activity was found in fractions that had affinity to antitransferrin. These fractions contained transferrin exclusively at pH 7.4, but additional protein fractions of albumin and alpha1-globulin mobility at pH 5.5.At pH 7.4 and 5.5, 10%–20% of the indium activity was detected in molecular fractions that had no affinity to antitransferrin. Immunologic analyses showed that these fractions contained transferrin. Why this transferrin did not bind to the antitransferrin remains unclear.In conclusion, In-113m can be used as an indicator of plasma proteins between pH 5.0 and 10.6.
DOI: 10.1007/BF01851974
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<record><TEI><teiHeader><fileDesc><titleStmt><title>Effects of pH on the stability of the indium-113m blood protein complex and the selective binding of indium-113m to transferrin</title><author><name>U. Hultkvist</name><affiliation wicri:level="1"><mods:affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</mods:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author><author><name>G. Westergren</name><affiliation wicri:level="1"><mods:affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</mods:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author><author><name>U. -B. Hansson</name><affiliation wicri:level="1"><mods:affiliation>Chemical Center, Biochemistry, Box 124, S-22100, Lund, Sweden</mods:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Chemical Center, Biochemistry, Box 124, S-22100, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author><author><name>L. Lewan</name><affiliation wicri:level="1"><mods:affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</mods:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="RBID">ISTEX:433_1987_Article_BF01851974.pdf</idno><date when="1987">1987</date><idno type="doi">10.1007/BF01851974</idno><idno type="wicri:Area/Main/Corpus">000167</idno><idno type="wicri:Area/Main/Curation">000167</idno><idno type="wicri:Area/Main/Exploration">000595</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Indium-113m</term><term>Microcirculation</term><term>PH stability</term><term>Transferrin</term><term>Vascular permeability</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="eng">Indium-113m (t1/2 = 100min; gamma-emission of 393keV) in trace amounts was injected i.v. in rats. Blood was collected by heart puncture 15 min after the injection, and blood plasma was separated by centrifugation. Gel filtration of plasma on Sephadex G-25M equilibrated with glycine/HCl (pH 2.2–3.6), NaHCO3/CO2 (pH 4.0–11.0) glycine/NaOH (pH 8.6–10.6) or sodium acetate/acetic acid (pH 3.0–5.0) was used to separate free indium from indium bound to macromolecular proteins. Determination of radioactivity in eluted fractions showed that more than 85% of the plasma indium was bound to macromolecules at pH values between 5.0 and pH 10.6. However, dissociation of the indium plasma protein complexes occurred at pH values below 5.5, and more than 90% of the indium radioactivity was found in the low molecular weight fraction at pH 2.2.Affinity chromatography using immobilized antibodies to rat transferrin was used to isolate transferrin at pH 7.4 and 5.5. Immunodiffusion and electrophoresis were used to identify the proteins in fractions obtained by affinity chromatography. It was found that the indium-113m activity was correlated with the content of transferrin and that 80%–90% of this activity was found in fractions that had affinity to antitransferrin. These fractions contained transferrin exclusively at pH 7.4, but additional protein fractions of albumin and alpha1-globulin mobility at pH 5.5.At pH 7.4 and 5.5, 10%–20% of the indium activity was detected in molecular fractions that had no affinity to antitransferrin. Immunologic analyses showed that these fractions contained transferrin. Why this transferrin did not bind to the antitransferrin remains unclear.In conclusion, In-113m can be used as an indicator of plasma proteins between pH 5.0 and 10.6.</div></front></TEI><mods xsi:schemaLocation="http://www.loc.gov/mods/v3 file:///applis/istex/home/loadistex/home/etc/xsd/mods.xsd" version="3.4" istexId="1c71599a5f6880b53b53a0e6ff12c9a744709eed"><titleInfo lang="eng"><title>Effects of pH on the stability of the indium-113m blood protein complex and the selective binding of indium-113m to transferrin</title></titleInfo><name type="personal"><namePart type="given">U.</namePart><namePart type="family">Hultkvist</namePart><role><roleTerm type="text">author</roleTerm></role><affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</affiliation></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Westergren</namePart><role><roleTerm type="text">author</roleTerm></role><affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</affiliation></name><name type="personal"><namePart type="given">U. -B.</namePart><namePart type="family">Hansson</namePart><role><roleTerm type="text">author</roleTerm></role><affiliation>Chemical Center, Biochemistry, Box 124, S-22100, Lund, Sweden</affiliation></name><name type="personal"><namePart type="given">L.</namePart><namePart type="family">Lewan</namePart><role><roleTerm type="text">author</roleTerm></role><affiliation>Dept. of Zoophysiology, Helgonavägen 3B, S-22362, Lund, Sweden</affiliation></name><typeOfResource>text</typeOfResource><genre>Original Papers</genre><genre>Original Paper</genre><originInfo><publisher>Springer-Verlag, Berlin/Heidelberg</publisher><dateCreated encoding="w3cdtf">1986-07-02</dateCreated><dateCaptured encoding="w3cdtf">1986-12-06</dateCaptured><dateValid encoding="w3cdtf">2005-05-28</dateValid><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="eng">Indium-113m (t1/2 = 100min; gamma-emission of 393keV) in trace amounts was injected i.v. in rats. Blood was collected by heart puncture 15 min after the injection, and blood plasma was separated by centrifugation. Gel filtration of plasma on Sephadex G-25M equilibrated with glycine/HCl (pH 2.2–3.6), NaHCO3/CO2 (pH 4.0–11.0) glycine/NaOH (pH 8.6–10.6) or sodium acetate/acetic acid (pH 3.0–5.0) was used to separate free indium from indium bound to macromolecular proteins. Determination of radioactivity in eluted fractions showed that more than 85% of the plasma indium was bound to macromolecules at pH values between 5.0 and pH 10.6. However, dissociation of the indium plasma protein complexes occurred at pH values below 5.5, and more than 90% of the indium radioactivity was found in the low molecular weight fraction at pH 2.2.Affinity chromatography using immobilized antibodies to rat transferrin was used to isolate transferrin at pH 7.4 and 5.5. Immunodiffusion and electrophoresis were used to identify the proteins in fractions obtained by affinity chromatography. It was found that the indium-113m activity was correlated with the content of transferrin and that 80%–90% of this activity was found in fractions that had affinity to antitransferrin. These fractions contained transferrin exclusively at pH 7.4, but additional protein fractions of albumin and alpha1-globulin mobility at pH 5.5.At pH 7.4 and 5.5, 10%–20% of the indium activity was detected in molecular fractions that had no affinity to antitransferrin. Immunologic analyses showed that these fractions contained transferrin. Why this transferrin did not bind to the antitransferrin remains unclear.In conclusion, In-113m can be used as an indicator of plasma proteins between pH 5.0 and 10.6.</abstract><subject lang="eng"><genre>Key words</genre><topic>Indium-113m</topic><topic>Transferrin</topic><topic>pH stability</topic><topic>Vascular permeability</topic><topic>Microcirculation</topic></subject><relatedItem type="series"><titleInfo type="abbreviated"><title>Res. Exp. Med.</title></titleInfo><titleInfo><title>Research in Experimental Medicine</title><partNumber>Year: 1987</partNumber><partNumber>Volume: 187</partNumber><partNumber>Number: 2</partNumber></titleInfo><genre>Archive Journal</genre><originInfo><dateIssued encoding="w3cdtf">1987-03-01</dateIssued><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><subject usage="primary"><topic>Medicine & Public Health</topic><topic>Internal Medicine</topic></subject><identifier type="issn">0300-9130</identifier><identifier type="issn">Electronic: 1433-8580</identifier><identifier type="matrixNumber">433</identifier><identifier type="local">IssueArticleCount: 8</identifier><recordInfo><recordOrigin>Springer-Verlag, 1987</recordOrigin></recordInfo></relatedItem><identifier type="doi">10.1007/BF01851974</identifier><identifier type="matrixNumber">Art6</identifier><identifier type="local">BF01851974</identifier><accessCondition type="use and reproduction">MetadataGrant: OpenAccess</accessCondition><accessCondition type="use and reproduction">AbstractGrant: OpenAccess</accessCondition><accessCondition type="restriction on access">BodyPDFGrant: Restricted</accessCondition><accessCondition type="restriction on access">BodyHTMLGrant: Restricted</accessCondition><accessCondition type="restriction on access">BibliographyGrant: Restricted</accessCondition><accessCondition type="restriction on access">ESMGrant: Restricted</accessCondition><part><extent unit="pages"><start>131</start><end>137</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1987</recordOrigin><recordIdentifier>433_1987_Article_BF01851974.pdf</recordIdentifier></recordInfo></mods></record>Pour manipuler ce document sous Unix (Dilib)
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