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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1990-8-13
|
| pubmed:abstractText |
The heat stability of beef myoglobin was investigated by means of its solubility and intensity of protein bands separated by isoelectric focusing. A method for the sensitive determination of myoglobin in the extracts was developed based on its ability to form a red dye by the oxidative coupling of 2,4-dichlorophenol and 4-aminoantipyrine in the presence of hydrogen peroxide. By this method, myoglobin could be determined to a concentration of 0.01 mg/ml. For the detection of electro-focused myoglobins, o-dianisidine has proved to be the most sensitive compound. The myoglobin content of the extracts, according to the intensity of the myoglobin bands in the electrophoretic gel, decreased with increasing temperature and heating-time. However, the position of the bands was not changed by the heat treatment.
|
| pubmed:language |
ger
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0044-3026
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
190
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
414-9
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1990
|
| pubmed:articleTitle |
[Effect of heat on the solubility and the electrophoretic behavior of myoglobin].
|
| pubmed:affiliation |
Bundesanstalt für Fleischforschung, Institut für Chemie und Physik, Kulmbach, Federal Republic of Germany.
|
| pubmed:publicationType |
Journal Article,
English Abstract,
Research Support, Non-U.S. Gov't
|