<p> A new technique for the systematic identification of metal-protein complexes combining gel chromatography with either neutron activation analysis or radioactive tracer methods has been proposed. The technique has been tested on the copper in serum situation to evaluate the results obtained on a well-known system.</p> <p> It was then applied to manganese in serum, manganese in erythrocytes and copper in erythrocytes. The results indicate that serum contains two manganese-binding proteins, one of low molecular weight and relatively labile in nature, the other of higher molecular weight and incorporating radioactive manganese in vivo at some definite time interval subsequent to the isotope's administration.</p> <p> Manganese in erythrocytes occurs as a porphyrin bound to apoglobin as a manganese analogue of hemoglobin.</p> <p> Copper in erythrocytes appears to exist in two forms - one firmly bound to erythrocuprein, the other more loosely bound to the same protein.</p> / Thesis / Doctor of Philosophy (PhD)
| Identifer | oai:union.ndltd.org:mcmaster.ca/oai:macsphere.mcmaster.ca:11375/17768 |
| Date | 03 1900 |
| Creators | Evans, David John Roy |
| Contributors | Fritze, K., Chemistry |
| Source Sets | McMaster University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis |
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