Preparation of histones by the use of Reinecke salt

Lindh, Nils Olof; Brantmark, B.

doi:10.1016/0003-2697(65)90310-6

Cited by 22 publications

(2 citation statements)

References 11 publications

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“…The column was washed with 5 volumes of the same buffer, and the histones were then removed from the column with 40% guanidine hydrochloride and 0.1 M sodium phosphate, pH 6.5. The fractions containing histones were combined and adjusted to 0.4 N HC1, and the histones were precipitated with Reinecke salt as previously described (Lindl & Brantmark, 1965). The precipitate was washed with acetone to remove the Reinecke salt, the pellet was dried, and the histones were resuspended in SDS sample buffer.…”

Section: Methodsmentioning

confidence: 99%

Exchange of histones H1, H2A, and H2B in vivo

Louters¹,

Chalkley²

1985

Biochemistry

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We have asked whether histones synthesized in the absence of DNA synthesis can exchange into nucleosomal structures. DNA synthesis was inhibited by incubating hepatoma tissue culture cells in medium containing 5.0 mM hydroxyurea for 40 min. During the final 20 min, the cells were pulsed with [3H]lysine to radiolabel the histones (all five histones are substantially labeled under these conditions). By two electrophoretic techniques, we demonstrate that histones H1, H2A, and H2B synthesized in the presence of hydroxyurea do not merely associate with the surface of the chromatin but instead exchange with preexisting histones so that for the latter two histones there is incorporation into nucleosome structures. On the other hand, H3 and H4 synthesized during this same time period appear to be only weakly bound, if at all, to chromatin. These two histones have been isolated from postnuclear washes and purified. Some possible implications of in vivo exchange are discussed.

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Section: Methodsmentioning

confidence: 99%

Exchange of histones H1, H2A, and H2B in vivo

Louters¹,

Chalkley²

1985

Biochemistry

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“…The supernatant was clarified by filtration through a no.-4-porosity sintered-glass funnel. Protein was next precipitated from the clear filtrate by the addition of Reinecke salt (ammonium tetrathiocyanodiammonochromate) (Lindh & Brantmark, 1965) and pelleted at 7000 g for 15 min. Pellets from the successive preparations were pooled, washed with acetone containing 60 mM-HCl and twice with acetone only, and dried under reduced pressure.…”

Section: Preparation Of Histone Himentioning

confidence: 99%

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

Vanfleteren¹,

Bun

Baere³

et al. 1990

Biochemical Journal

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The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.

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Preparation and Analysis of Basic Proteins

Lindh

Brantmark

1966

Methods of Biochemical Analysis

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Preparation of histones by the use of Reinecke salt

Cited by 22 publications

References 11 publications

Exchange of histones H1, H2A, and H2B in vivo

Exchange of histones H1, H2A, and H2B in vivo

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

Preparation and Analysis of Basic Proteins

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