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Inhibition of ADP-ribosylation of histone H1 by analogs of diadenosine 5′, 5‴-p1,p4-tetraphosphate

✍ Scribed by Hisanori Suzuki; Yasuharu Tanaka; Daniela Tornese Buonamassa; Benedetta Farina; Enzo Leone

Book ID
104669983
Publisher
Springer
Year
1987
Tongue
English
Weight
260 KB
Volume
74
Category
Article
ISSN
0300-8177

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✦ Synopsis

The effects of analogs of diadenosine 5',5'''-p1,p4-tetraphosphate (Ap4A) were examined on the ADP-ribosylation reaction of histone H1 catalysed by purified bovine thymus poly(ADP-ribose)transferase. Among the compounds tested, epsilon Ap4A and ApCH2pppA were shown to be the most efficient inhibitors of the enzyme. From kinetic studies of their action, it appears that epsilon Ap4A and ApCH2pppA might be 'mixed type' inhibitors.

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Determination of diadenosine 5′,5‴,-P1,P
Determination of diadenosine 5′,5‴,-P1,P4-tetraphosphate levels in cultured mammalian cells
✍ Jeffrey C. Baker; Myron K. Jacobson 📂 Article 📅 1984 🏛 Elsevier Science 🌐 English ⚖ 846 KB

A simple method for measuring the cellular content of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) in cultured mammalian cells is described. Ap4A was rapidly extracted by dissolving cell monolayers using 0.1 N NaOH. It was separated from the bulk of cellular components in a single step by selecti