NDLI: The existence and properties of two dimers of rat liver ecto-5'-nucleotidase.

Content Provider	PubMed Central
Author	Bailyes, E. M. Soos, M. Jackson, P. Newby, A. C. Siddle, K. Luzio, J. P.
Abstract	Immunoaffinity-purified rat liver 5'-nucleotidase contained two subunits of Mr 70 000 (alpha) and 38 000 (beta). Charge-shift electrophoresis and chemical cross-linking revealed that approx. 80% of the solubilized enzyme activity occurred as an alpha alpha-dimer of Mr 140 000. The remaining 20% was an alpha beta-dimer of Mr 108 000. The beta-subunit did not possess enzymic activity. Peptide mapping and immunoblotting with antibodies against the alpha- and beta-subunits showed that the beta-subunit was homologous with a part of the alpha-subunit. Three monoclonal antibodies against rat liver 5'-nucleotidase were characterized as binding to the extracellular domain of the enzyme. All three monoclonal antibodies and concanavalin A bound to the alpha-subunit, but no binding could be detected to the beta-subunit. It was therefore concluded that the beta-subunit was a fragment of an alpha-subunit that had lost an extracellular domain. Both forms of the enzyme occurred in freshly solubilized membrane preparations as well.
Starting Page	369
File Format	PDF
ISSN	14708728
e-ISSN	14708728
Journal	Biochemical Journal
Issue Number	2
Volume Number	221
Language	English
Publisher Date	1984-07-15
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Biochemistry

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The existence and properties of two dimers of rat liver ecto-5'-nucleotidase.