File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Chemical cross-linking of hemoglobin H. A possible approach to introduce cooperativity and modification of its oxygen transport properties

TitleChemical cross-linking of hemoglobin H. A possible approach to introduce cooperativity and modification of its oxygen transport properties
Authors
Issue Date1979
Citation
Biochimica Et Biophysica Acta, 1979, v. 580 n. 1, p. 75-84 How to Cite?
AbstractNative and reconstituted hemoglobin H molecules were cross-linked with glutaraldehyde at pH values close to the physiological. The Schiff base adducts were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis before and after reduction with sodium borohydride. The major component had a molecular weight of about 31 000 which corresponded to the dimeric species of the β subunit. In contrast to the native protein, which has very high oxygen affinity and no heme-heme interaction or 2,3-diphosphoglyceric acid effect, the modified hemoglobin H molecules showed cooperative oxygen binding, decreased oxygen affinity and a noticeable 2,3-diphosphoglyceric acid effect.
Persistent Identifierhttp://hdl.handle.net/10722/147300
ISSN
1999 Impact Factor: 2.59
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTam, JWOen_US
dc.contributor.authorCheng, LYen_US
dc.date.accessioned2012-05-29T06:02:47Z-
dc.date.available2012-05-29T06:02:47Z-
dc.date.issued1979en_US
dc.identifier.citationBiochimica Et Biophysica Acta, 1979, v. 580 n. 1, p. 75-84en_US
dc.identifier.issn0006-3002en_US
dc.identifier.urihttp://hdl.handle.net/10722/147300-
dc.description.abstractNative and reconstituted hemoglobin H molecules were cross-linked with glutaraldehyde at pH values close to the physiological. The Schiff base adducts were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis before and after reduction with sodium borohydride. The major component had a molecular weight of about 31 000 which corresponded to the dimeric species of the β subunit. In contrast to the native protein, which has very high oxygen affinity and no heme-heme interaction or 2,3-diphosphoglyceric acid effect, the modified hemoglobin H molecules showed cooperative oxygen binding, decreased oxygen affinity and a noticeable 2,3-diphosphoglyceric acid effect.en_US
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Actaen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshChemical Phenomenaen_US
dc.subject.meshChemistryen_US
dc.subject.meshCross-Linking Reagentsen_US
dc.subject.meshGlutaralen_US
dc.subject.meshHemoglobin H - Metabolismen_US
dc.subject.meshHemoglobins, Abnormal - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshOxygen - Blooden_US
dc.subject.meshProtein Bindingen_US
dc.titleChemical cross-linking of hemoglobin H. A possible approach to introduce cooperativity and modification of its oxygen transport propertiesen_US
dc.typeArticleen_US
dc.identifier.emailCheng, LY:lcheng@hkucc.hku.hken_US
dc.identifier.authorityCheng, LY=rp00317en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid121058-
dc.identifier.scopuseid_2-s2.0-0018693627en_US
dc.identifier.volume580en_US
dc.identifier.issue1en_US
dc.identifier.spage75en_US
dc.identifier.epage84en_US
dc.identifier.isiWOS:A1979HQ37900008-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridTam, JWO=7102534616en_US
dc.identifier.scopusauthoridCheng, LY=7403337122en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats