Affinity purification of active subunit 1 of herpes simplex virus type 1 ribonucleotide reductase exhibiting a protein kinase activity

Herpes simplex virus (HSV) ribonucleotide reductase is formed by the association of two distinct dimeric subunits, R1 and R2. Attempts to purify either the HSV holoenzyme or its R1 subunit in their active form have been unsuccessful until now. The C terminus of the R2 protein being involved in the a...

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Veröffentlicht in:The Journal of biological chemistry 1991-05, Vol.266 (15), p.9647-9651
Hauptverfasser: PARADIS, H, GAUDREAU, P, MASSIE, B, LAMARCHE, N, GUILBAULT, C, GRAVEL, S, LANGELIER, Y
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Sprache:eng
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