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Physicochemical and immunological studies on mammalian 5'-deoxy-5'-methylthioadenosine phosphorylase (Articolo in rivista)

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Physicochemical and immunological studies on mammalian 5'-deoxy-5'-methylthioadenosine phosphorylase (Articolo in rivista) (literal)

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Della Ragione, F., Oliva, A., Gragnaniello, V., Russo, G.L., Palumbo, R., Zappia, V. (1990)
Physicochemical and immunological studies on mammalian 5'-deoxy-5'-methylthioadenosine phosphorylase
in The Journal of biological chemistry (Print); American society for biochemistry and molecular biology, Baltimore (Stati Uniti d'America)
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Della Ragione, F., Oliva, A., Gragnaniello, V., Russo, G.L., Palumbo, R., Zappia, V. (literal)

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cited By (since 1996)14 Questa pubblicazione si riferisce a un periodo in cui gli autori non lavoravano presso il CNR PDF scaricabile gratuitamente al sito: http://www.jbc.org/content/265/11/6241.short (literal)

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Institute of Biochemistry of Macromolecules, First Medical School, University of Naples, Naples 80138, Italy (literal)

Titolo

Physicochemical and immunological studies on mammalian 5'-deoxy-5'-methylthioadenosine phosphorylase (literal)

Abstract

5'-Deoxy-5'-methylthioadenosine phosphorylase (MTAase) was purified to homogeneity (10,000-fold) from bovine liver with a recovery of 12%. The pure protein shows a molecular weight of about 98,000 ± 3,000 and is composed of three apparently identical subunits. Several physicochemical features have been investigated including hydrodynamic properties, amino acid composition, and secondary structure. In particular, the CD spectrum of the protein indicates a very low ?-helical content and a large percent of ?-structure and random coil. The pure protein was used to raise specific rabbit antisera but, because of the scarce antigenic properties of the native enzyme, different chemically modified forms were prepared and employed as immunogens. Among the antibodies obtained, those to keyhole limpet hemocyanin-MTAase recognize both the native and the denatured enzyme and are also active against the human protein. Therefore, they were employed as a tool to investigate the occurrence of inactive forms of MTAase in two human malignant cell lines lacking this enzymatic activity. The results obtained with K562 and Jurkat cells indicate that the protein is absent in these phosphorylase-deficient cell lines. (literal)

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