Factors affecting the binding of cyanocobalamin to serum proteins from various animals
Identifieur interne : 005356 ( Istex/Checkpoint ); précédent : 005355; suivant : 005357Factors affecting the binding of cyanocobalamin to serum proteins from various animals
Auteurs : Harold L. Rosenthal [États-Unis] ; Gloria O'Brien [États-Unis] ; Shirley Austin [États-Unis]Source :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1962.
Abstract
The cyanocobalamin protein complex of animal sera is associated with various protein fractions ranging from α1-globulin in chicken serum to β-globulins for human serum. Equilibrium dialysis studies indicate the presence of more than one major binding site in serum from man, dog, rabbit, frog, and chicken.The binding of cyanocobalamin to human, dog, and rabbit serum is eliminated by treatment of serum with 8 M urea. This effect is partially reversible for rabbit serum but is irreversible for human and dog serum. Cyanocobalamin bound to serum prior to urea treatment affords complete protection except for rabbit serum. The cyanocobalamin-binding capacity of frog and chicken serum is not affected by urea treatment. Reduction with hydrogen, catalyzed with palladium, depresses the cyanocobalamin binding in dog serum, while reduction with thioglycolate is ineffective for all sera tested. Oxidation with periodate depresses the binding capacity of human and dog serum more than sera from rabbit, frog, or chicken, while oxidation with copper chloride and hydrogen peroxide yields results opposite to that of periodate.The data are consistent with the concept that the cyanocobalamin-binding phenomena in sera is associated with multiple binding sites that may be different for various animal species and that specific spatial orientation between the protein and cyanocobalamin moieties is necessary for binding to occur.
Url:
DOI: 10.1016/0003-9861(62)90017-6
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Rosenthal</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>From the Department of Physiological Chemistry, Washington University School of Dentistry, St. Louis, Missouri</wicri:regionArea><placeName><region type="state">Missouri (État)</region></placeName></affiliation></author><author><name sortKey="O Brien, Gloria" sort="O Brien, Gloria" uniqKey="O Brien G" first="Gloria" last="O'Brien">Gloria O'Brien</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>From the Department of Physiological Chemistry, Washington University School of Dentistry, St. Louis, Missouri</wicri:regionArea><placeName><region type="state">Missouri (État)</region></placeName></affiliation></author><author><name sortKey="Austin, Shirley" sort="Austin, Shirley" uniqKey="Austin S" first="Shirley" last="Austin">Shirley Austin</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>From the Department of Physiological Chemistry, Washington University School of Dentistry, St. Louis, Missouri</wicri:regionArea><placeName><region type="state">Missouri (État)</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1962">1962</date><biblScope unit="volume">99</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="319">319</biblScope><biblScope unit="page" to="325">325</biblScope></imprint><idno type="ISSN">0003-9861</idno></series><idno type="istex">15517A47FCFD56C4534BF61C737E965D76BFFC59</idno><idno type="DOI">10.1016/0003-9861(62)90017-6</idno><idno type="PII">0003-9861(62)90017-6</idno><idno type="ArticleID">62900176</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The cyanocobalamin protein complex of animal sera is associated with various protein fractions ranging from α1-globulin in chicken serum to β-globulins for human serum. Equilibrium dialysis studies indicate the presence of more than one major binding site in serum from man, dog, rabbit, frog, and chicken.The binding of cyanocobalamin to human, dog, and rabbit serum is eliminated by treatment of serum with 8 M urea. This effect is partially reversible for rabbit serum but is irreversible for human and dog serum. Cyanocobalamin bound to serum prior to urea treatment affords complete protection except for rabbit serum. The cyanocobalamin-binding capacity of frog and chicken serum is not affected by urea treatment. Reduction with hydrogen, catalyzed with palladium, depresses the cyanocobalamin binding in dog serum, while reduction with thioglycolate is ineffective for all sera tested. Oxidation with periodate depresses the binding capacity of human and dog serum more than sera from rabbit, frog, or chicken, while oxidation with copper chloride and hydrogen peroxide yields results opposite to that of periodate.The data are consistent with the concept that the cyanocobalamin-binding phenomena in sera is associated with multiple binding sites that may be different for various animal species and that specific spatial orientation between the protein and cyanocobalamin moieties is necessary for binding to occur.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Missouri (État)</li></region></list><tree><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Rosenthal, Harold L" sort="Rosenthal, Harold L" uniqKey="Rosenthal H" first="Harold L." last="Rosenthal">Harold L. Rosenthal</name></region><name sortKey="Austin, Shirley" sort="Austin, Shirley" uniqKey="Austin S" first="Shirley" last="Austin">Shirley Austin</name><name sortKey="O Brien, Gloria" sort="O Brien, Gloria" uniqKey="O Brien G" first="Gloria" last="O'Brien">Gloria O'Brien</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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