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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein.

Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. Purification of PARG from many tissues revealed heterogeneity in activity and structure of this enzyme. To investigate PARG structure and localization, we developed a highly sensitive one-dimensional zymogram allowing us to analyze PARG activity in crude extracts of Cos-7, Jurkat, HL-60, and Molt-3 cells. In all extracts, a single PARG activity band corresponding to a protein of about 110 kDa was detected. This 110-kDa PARG activity was found mainly in cytoplasmic rather than in nuclear extracts of Cos-7 cells.[1]

References

  1. Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein. Winstall, E., Affar, E.B., Shah, R., Bourassa, S., Scovassi, A.I., Poirier, G.G. Exp. Cell Res. (1999) [Pubmed]
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