A method is described for the assay of histone methyltransferase using soluble histones as substrate. The precipitation of the methylated protein on chromatography paper allows for greater sensitivity and more rapid sample processing than have previously been reported. After incubation of the enzyme
A more sensitive assay for histone deacetylase
โ Scribed by Jaap H. Waterborg; Harry R. Matthews
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 425 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
The new assay uses as substrate a peptide derived from the amino terminal domain of calf histone H4. The peptide contains all the lysines that are acetylated in H4 in vivo and these lysines are specifically labeled in vitro with acetic anhydride to a high specific activity. This substrate allows histone deacetylase activity to be measured economically and with high sensitivity either with pure enzyme or with crude extracts.
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Recent years have brought an enormous increase in knowledge concerning the involvement of histone deacetylase (HDAC) in gene regulation and the potential use of its inhibitors in transcription therapy. This also stimulates research toward new methods for the determination of HDAC activity and thus t
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