Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2000-9-25
pubmed:abstractText
Hemoglobin-mediated lipid oxidation was studied by adding hemolysate to washed cod muscle. Three pH values were examined (pH 7.6, 7.2, and 6.0). The lag time prior to rancidity and thiobarbituric acid reactive substance development decreased greatly as the pH was reduced (p < 0.01). Formation of methemoglobin due to autoxidation of the heme pigment was found to occur more rapidly at reduced pH. Also, the level of deoxyhemoglobin was found to sharply increase with pH reduction in the range of pH 7.6-6.0. This suggested a potential role for deoxyhemoglobin as a catalyst. ATP lowered hemoglobin oxygenation at pH 7.2. Peroxidation of linoleic acid by oxy/deoxyhemoglobin and methemoglobin was investigated at two levels of preformed lipid hydroperoxides. At a reduced level of preformed lipid hydroperoxides, oxy/deoxyhemoglobin stimulated peroxidation of linoleic acid, whereas methemoglobin did not. At the higher level of preformed lipid hydroperoxides, both oxy/deoxyhemoglobin and methemoglobin were active. This investigation suggests that reduced hemoglobins played an important role in lipid oxidation processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3141-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Effect of pH on lipid oxidation using trout hemolysate as a catalyst: a possible role for deoxyhemoglobin.
pubmed:affiliation
Massachusetts Agricultural Experiment Station, Department of Food Science, University of Massachusetts/Amherst Marine Station, Gloucester 01930, USA. mrichard@foodsci.umass.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't