Our findings suggest that although deep CMBs are mainly linked to subcortical SVD, both subcortical SVD and amyloid-related pathologies (eg, CAA) contribute to the pathogenesis of lobar CMBs, at least in subjects with mixed lobar and deep CMBs. Furthermore, subcortical SVD and amyloid-related pathologies interact to increase the risk of lobar CMBs.
Two soluble forms of novel glutamate dehydrogenase isoproteins, designated GDH I and GDH 11, have been purified from bovine brain. GDH I and GDH I1 were separated on a hydroxyapatite column and eluted by a step gradient at different phosphate concentrations (30 mM and 50 rnM for GDH I and GDH 11, respectively). The preparations were homogeneous on SDS/PAGE. GDH I and GDH II showed similarity in their molecular sizes and are composed of six identical subunits having a molecular size of 57500 Da. Differences between the biochemical properties of GDH I and GDH 11, such as N-terminal amino acid sequences of intact and tryptic-digested enzymes, kinetic parameters, optimum pH and heat stability, were extensively examined in both reductive amination of a-oxoglutarate and oxidative deamination of glutamate. The different effects of ADP on GDH isoproteins were also studied under various conditions. These results indicate that GDH I and GDH 11, isolated from bovine brain, are novel and distinct polypeptides.
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