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Oxidative and reductive reactions of sulphhaemoglobin with various reagents correlated with changes in quaternary structure of the protein.
The absorption maxima in the Soret region and near 620nm of sulphhaemoglobin shifted from 419.5nm to 423nm and from 623nm to 619nm respectively with a decrease in oxygen concentrations of the sulphhaemoglobin solution [101.3, 20.3 and 0 kPa (760, 152 and 0 mmHg) partial pressures]. The major changes...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1984
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1144085/ https://ncbi.nlm.nih.gov/pubmed/6477486 |
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