AI Article Synopsis
- Adenosine deaminase has been isolated and purified from various brain regions, revealing important biochemical characteristics.
- The enzyme shows heterogeneity based on gel filtration and electrophoresis results, indicating different forms or variants.
- Cu2+ is the only metal ion that irreversibly inhibits the enzyme activity across all preparations, while the enzyme's function does not depend on any essential SH-group.
Article Abstract
Adenosine deaminase from the white and gray matter of the large hemispheres, cerebellum, medulla oblongata and pituitary anterior lobe has been isolated and purified. The pH optimum, Km, molecular mass, yield and specific activities for all the enzyme preparations have been determined. Gel filtration and electrophoresis data point to the heterogeneity of the enzyme. The lack of effects of SH-reagents suggests the absence of an essential SH-group. Among five bivalent metal ions, only Cu2+ irreversibly inhibited the enzyme activity in all the preparations.
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