Show simple item record

dc.creatorNiketić, Vesna
dc.creatorTomašević, N
dc.creatorVajs, Vlatka
dc.creatorBojić, Ž
dc.date.accessioned2019-05-01T09:14:41Z
dc.date.available2019-05-01T09:14:41Z
dc.date.issued1996
dc.identifier.issn0352-5139
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/2794
dc.description.abstractIn this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.en
dc.publisherSerbian Chemical Society
dc.rightsopenAccess
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceJournal of the Serbian Chemical Society
dc.subjectGlycophospholipid
dc.subjectHemoglobin
dc.subjectInsulin
dc.titleCovalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulinen
dc.typearticleen
dc.rights.licenseBY-NC-ND
dcterms.abstractТомашевић, Н; Вајс, Влатка; Никетић, Весна; Бојић, Ж;
dc.citation.volume61
dc.citation.issue7
dc.citation.spage535
dc.citation.epage538
dc.identifier.scopus2-s2.0-0041357184
dc.type.versionpublishedVersion


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record