Show simple item record

dc.contributor.author Bonaventura, J
dc.contributor.author Rodriguez, EN
dc.contributor.author Beyley, V
dc.contributor.author Vega, IE
dc.coverage.spatial United States
dc.date.accessioned 2011-04-15T16:46:29Z
dc.date.issued 2010-08
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20553188
dc.identifier.citation J Med Food, 2010, 13 (4), pp. 943 - 949
dc.identifier.uri http://hdl.handle.net/10161/3325
dc.description.abstract Recent studies have shown that deoxygenated human red blood cells (RBCs) converted garlic-derived polysulfides into hydrogen sulfide, which in turn produced vasorelaxation in aortic ring preparations. The vasoactivity was proposed to occur via glucose- and thiol-dependent acellular reactions. In the present study, we investigated the interaction of garlic extracts with human deoxygenated RBCs and its effect on intracellular hemoglobin molecules. The results showed that garlic extract covalently modified intraerythrocytic deoxygenated hemoglobin. The modification identified consisted of an addition of 71 atomic mass units, suggesting allylation of the cysteine residues. Consistently, purified human deoxyhemoglobin reacted with chemically pure diallyl disulfide, showing the same modification as garlic extracts. Tandem mass spectrometry analysis demonstrated that garlic extract and diallyl disulfide modified hemoglobin's beta-chain at cysteine-93 (beta-93C) or cysteine-112 (beta-112C). These results indicate that garlic-derived organic disulfides as well as pure diallyl disulfide must permeate the RBC membrane and modified deoxyhemoglobin at beta-93C or beta-112C. Although the physiological role of the reported garlic extract-induced allyl modification on human hemoglobin warrants further study, the results indicate that constituents of natural products, such as those from garlic extract, modify intracellular proteins.
dc.format.extent 943 - 949
dc.language ENG
dc.language.iso en_US en_US
dc.relation.ispartof J Med Food
dc.relation.isversionof 10.1089/jmf.2009.0258
dc.subject Erythrocytes
dc.subject Garlic
dc.subject Hemoglobins
dc.subject Humans
dc.subject Plant Extracts
dc.subject Protein Processing, Post-Translational
dc.title Allylation of intraerythrocytic hemoglobin by raw garlic extracts.
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-8-0 en_US
duke.description.endpage 949 en_US
duke.description.issue 4 en_US
duke.description.startpage 943 en_US
duke.description.volume 13 en_US
dc.relation.journal Journal of Medicinal Food en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20553188
pubs.issue 4
pubs.organisational-group /Duke
pubs.organisational-group /Duke/Nicholas School of the Environment
pubs.organisational-group /Duke/Nicholas School of the Environment/Marine Science and Conservation
pubs.publication-status Published
pubs.volume 13
dc.identifier.eissn 1557-7600

Files in this item

This item appears in the following Collection(s)

Show simple item record