|
KMID : 1161420100130040943
|
|
Journal of Medicinal Food
2010 Volume.13 No. 4 p.943 ~ p.949
|
|
|
Allylation of Intraerythrocytic Hemoglobin by Raw Garlic Extracts
|
|
Bonaventura Joseph
Rodriguez Eva N.
Beyley Veronica
Vega Irving E.
|
|
|
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 (β-93C) or cysteine-112 (β-112C). These results indicate that garlic-derived organic disulfides as well as pure diallyl disulfide must permeate the RBC membrane and modified deoxyhemoglobin at β-93C or β-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.
|
|
|
KEYWORD
|
|
|
diallyl disulfide, garlic extract, hemoglobin, posttranslational modification, red blood cells
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
 
|