[After care of breast carcinoma].
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Biomedical subjects
Publications and source records attributed to E Blum.
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The alpha-galactosidase A activity from fibroblasts of five Fabry patients and five controls has been separated from alpha-galactosidase B through small DEAE-cellulose columns and in some experiments by treatment of the fibroblast extracts with Sepharose coupled to anti-alpha-galactosidase B antibodies. By these independent methods, it has been shown that there is a residual alpha-galactosidase A in Fabry's disease, which is immunologically similar to the alpha-galactosidase A from the controls. The alpha-galactosidase A from all of the patients and controls has the same apparent Km value for the synthetic substrate 4-methylumbelliferyl-alpha-galactosidase A, while the fifth has a thermolabile enzyme like that from the controls. The amount of immunologically active alpha-galactosidase A seems to be decreased in the patients tested.
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Activities of the oligomeric enzymes urease and l-glutamate dehydrogenase were measured after exposure as dry preparations to various doses of electron radiation. Inactivation curves were exponential. ;Target sizes' deduced from these were small compared with the molecular weights of the whole enzyme molecules, but accorded well with independent estimates of the sizes of functional subunits. It was concluded that, when these were in associated from, there could be no transfer of absorbed energy between subunits.
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