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Differentiating the effects of microwave and heat on tissue proteins and their crosslinking by formaldehyde

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Summary

Alkaline phosphatase activity in mouse liver blocks, cooled by an ice-bath, decreased by 50% in 5 min of microwave irradiation (280 W). This loss of protein tertiary structure has been mirrored by ultrastructural changes in the same tissue. Microwave irradiation did not produce clevage or polymerization of lysozyme or haemoglobin. Protein formaldehyde reaction mixtures produced protein polymers between 0° and 40°C which could be separated by SDS-polyacrylamide gel electrophoresis. Microwave irradiation of lysozyme or haemoglobin plus formaldehyde on icebath up to 30 min produced a similar electrophoretic pattern. When lysozyme or haemoglobin plus formaldehyde was heated to 60°C for 30 min, the protein polymers migrated faster on electrophoresis, suggesting a smaller hydrodynamic volume than expected due to intramolecular crosslink formation, not opened up under the conditions of electrophoresis.

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Authors and Affiliations

  1. Department of Pathology, Ninewells Hospital and Medical School, Dundee, UK

    D. Hopwood, G. Yeaman & G. Milne

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  1. D. Hopwood
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  2. G. Yeaman
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  3. G. Milne
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Hopwood, D., Yeaman, G. & Milne, G. Differentiating the effects of microwave and heat on tissue proteins and their crosslinking by formaldehyde. Histochem J 20, 341–346 (1988). https://doi.org/10.1007/BF01002727

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  • DOI: https://doi.org/10.1007/BF01002727

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