Effect of synthetic carrier ampholytes on saturation of human serum transferrin.
Identifieur interne : 000049 ( Pmc/Corpus ); précédent : 000048; suivant : 000050Effect of synthetic carrier ampholytes on saturation of human serum transferrin.
Auteurs : A. Oratore ; A M D'Alessandro ; G. D'AndreaSource :
- Biochemical Journal [ 0264-6021 ] ; 1989.
Abstract
We have investigated the effect in solution of synthetic carrier ampholytes on the saturation of human serum transferrin. By spectrophotometric titrations of human serum transferrin with various Fe3+-carrier ampholyte solutions, we demonstrated that under these conditions carrier ampholytes behave as typical chelators, their binding curves being very similar to that obtained with disodium nitrilotriacetate. On performing titration experiments at three different pH values, carrier ampholytes act like nitrilotriacetate at pH 7.5, but the former are more effective iron donors at pH 8.4 and worse iron donors at pH 5.2. Spectrophotometric titrations of isolated C-terminal and N-terminal fragments obtained from human serum transferrin by thermolysin cleavage show no differences between them, and no differences with respect to the whole protein except that they contain half the number of binding sites. In order to determine a site-specificity of iron in the presence of ampholytes, the classical urea/polyacrylamide-gel-electrophoresis technique was adopted. Under saturating conditions carrier ampholyte solutions act mostly on the C-terminal site, whereas desaturating agents remove iron preferentially from the N-terminal site. Our findings support the hypothesis that Ampholine may chelate Fe3+ as well as many other compounds.
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PubMed: 2730592
PubMed Central: 1138604
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PMC:1138604Le document en format XML
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<author><name sortKey="D Alessandro, A M" sort="D Alessandro, A M" uniqKey="D Alessandro A" first="A M" last="D'Alessandro">A M D'Alessandro</name>
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<series><title level="j">Biochemical Journal</title>
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<front><div type="abstract" xml:lang="en"><p>We have investigated the effect in solution of synthetic carrier ampholytes on the saturation of human serum transferrin. By spectrophotometric titrations of human serum transferrin with various Fe3+-carrier ampholyte solutions, we demonstrated that under these conditions carrier ampholytes behave as typical chelators, their binding curves being very similar to that obtained with disodium nitrilotriacetate. On performing titration experiments at three different pH values, carrier ampholytes act like nitrilotriacetate at pH 7.5, but the former are more effective iron donors at pH 8.4 and worse iron donors at pH 5.2. Spectrophotometric titrations of isolated C-terminal and N-terminal fragments obtained from human serum transferrin by thermolysin cleavage show no differences between them, and no differences with respect to the whole protein except that they contain half the number of binding sites. In order to determine a site-specificity of iron in the presence of ampholytes, the classical urea/polyacrylamide-gel-electrophoresis technique was adopted. Under saturating conditions carrier ampholyte solutions act mostly on the C-terminal site, whereas desaturating agents remove iron preferentially from the N-terminal site. Our findings support the hypothesis that Ampholine may chelate Fe3+ as well as many other compounds.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochem J</journal-id>
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<title-group><article-title>Effect of synthetic carrier ampholytes on saturation of human serum transferrin.</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Oratore</surname>
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<contrib contrib-type="author"><name><surname>D'Alessandro</surname>
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<contrib contrib-type="author"><name><surname>D'Andrea</surname>
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<aff>Departimento di Scienze, Università degli Studi dell'Aquila degli Abruzzi, Italy.</aff>
<pub-date pub-type="ppub"><day>1</day>
<month>5</month>
<year>1989</year>
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<volume>259</volume>
<issue>3</issue>
<fpage>909</fpage>
<lpage>912</lpage>
<abstract><p>We have investigated the effect in solution of synthetic carrier ampholytes on the saturation of human serum transferrin. By spectrophotometric titrations of human serum transferrin with various Fe3+-carrier ampholyte solutions, we demonstrated that under these conditions carrier ampholytes behave as typical chelators, their binding curves being very similar to that obtained with disodium nitrilotriacetate. On performing titration experiments at three different pH values, carrier ampholytes act like nitrilotriacetate at pH 7.5, but the former are more effective iron donors at pH 8.4 and worse iron donors at pH 5.2. Spectrophotometric titrations of isolated C-terminal and N-terminal fragments obtained from human serum transferrin by thermolysin cleavage show no differences between them, and no differences with respect to the whole protein except that they contain half the number of binding sites. In order to determine a site-specificity of iron in the presence of ampholytes, the classical urea/polyacrylamide-gel-electrophoresis technique was adopted. Under saturating conditions carrier ampholyte solutions act mostly on the C-terminal site, whereas desaturating agents remove iron preferentially from the N-terminal site. Our findings support the hypothesis that Ampholine may chelate Fe3+ as well as many other compounds.</p>
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