Abstract：
:We have identified a phosphoprotein phosphatase which dephosphorylates efficiently the NC protein of coronavirus JHM. The activity was found in L-2 murine fibroblasts, Wistar Furth rat neonatal brain extracts, Wistar Furth rat oligodendrocyte primary cells and in Roc-1 cells, an oligodendrocytic hybrid cell line. In both L-2 cells and Roc-1 cells the enzyme was found to be localized predominantly in the endosomal fraction. The enzyme is optimally active at pH 7.0 and has a requirement for Mn++ ions. This PPPase activity is distinguishable from acidic and alkaline phosphatases. In view of the specificity of the endosomal PPPase for the phosphory-lated NC protein it is hypothesized that this enzyme may have a function during early stages of coronavirus infection.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Mohandas DV,Dales Sdoi
10.1007/978-1-4684-5823-7_35subject
Has Abstractpub_date
1990-01-01 00:00:00pages
255-60eissn
0065-2598issn
2214-8019journal_volume
276pub_type
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