dc.contributor.author
Mezquita Pla, Jovita
dc.contributor.author
Chiva i Royo, Manuel
dc.contributor.author
Vidal Malaka, Santiago
dc.contributor.author
Mezquita Pla, Cristóbal
dc.date.issued
2021-05-31T15:29:03Z
dc.date.issued
2021-05-31T15:29:03Z
dc.date.issued
1982-03-11
dc.date.issued
2021-05-31T15:29:03Z
dc.identifier
https://hdl.handle.net/2445/177832
dc.description.abstract
We have used a method previously described by Reeves and Candido (1) to partially release histone deacetylase from cell nuclei together with putative regulators of the enzyme. Histone deacetylase released from testis cell nuclei and its putative regulators were separated by gel filtration in Sepharose 6B. A peak of low molecular weight contains a heat-stable factor that stimulate histone deacetylase in vitro. Many of the properties of the activator coincide with those of the protein HMG-20 (ubiquitin). Ubiquitin isolated from testis cell nuclei stimulated histone deacetylase in vitro. It has been suggested that HMG-17 partially inhibits histone deacetylase in Fried cell nuclei (2). In our system, HMG-17 shows no inhibitory effect on histone deacetylase activity.
dc.format
application/pdf
dc.publisher
Oxford University Press
dc.relation
Reproducció del document publicat a: https://doi.org/10.1093/nar/10.5.1781
dc.relation
Nucleic Acids Research, 1982, vol. 10, num. 5, p. 1781-1797
dc.relation
https://doi.org/10.1093/nar/10.5.1781
dc.rights
cc-by-nc (c) Mezquita Pla, Jovita et al., 1982
dc.rights
https://creativecommons.org/licenses/by-nc/4.0/
dc.rights
info:eu-repo/semantics/openAccess
dc.source
Articles publicats en revistes (Ciències Fisiològiques)
dc.title
Effect of high mobility group nonhistone proteins HMG-20 (ubiquitin) and HMG-17 on histone deacetylase activity assayed in vitro
dc.type
info:eu-repo/semantics/article
dc.type
info:eu-repo/semantics/publishedVersion
