The activities of the hexose monophosphate pathway enzymes glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were measured at autopsy in control and Alzheimer's disease brains. Enzyme activities did not vary between different areas of brain and were unaltered by age. In Alzheimer's disease, the activities of both enzymes were increased, the glucose-6-phosphate dehydrogenase activity being almost double the activity of normal controls. We propose that this increased enzyme activity is a response to elevated brain peroxide metabolism.
1H- and 13C-n.m.r. measurements enable direct observation of the rate of formation of dehydroalanine residues resulting from lysis of the disulphide bonds of insulin and oxidized glutathione in base at pD13. The data provide clear evidence for the beta-elimination mechanism for this reaction. The dehydroalanine-containing products from the lysis of insulin undergo secondary reactions.
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