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Topography, purification and characterization of thyroidal 5'-nucleotidase
C Peeters1, M de Wolf, G Van Dessel
1RUCA-Laboratory for Human Biochemistry, University of Antwerp, Belgium.
The International Journal of Biochemistry
|January 1, 1988
Abstract:
1. Subcellular studies of bovine thyroid indicate that 5'-nucleotidase is predominantly associated with plasma membranes, although a considerable part of this ectoenzyme is also found internalized. 2. The enzyme displaying the features of a glycoprotein has been purified 1400 times by detergent solubilization and two subsequent affinity chromatographic steps. 3. Thyroidal 5'-nucleotidase can be classified as an unspecific metallo-dependent 5'-ribonucleotide phosphohydrolase. The native enzyme exists as a dimer (MW 150 kDalton), composed of two similar or identical subunits.