Separation of histones by reverse-phase high-performance liquid chromatography: Analysis of the binding of carcinogens to histones

Kurokawa, Mineo; MacLeod, Michael C.

doi:10.1016/0003-2697(85)90082-x

Cited by 25 publications

(8 citation statements)

References 30 publications

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“…, both variants Hla and Hlb show higher valine and lower alanine contents compared with the variants HIc, HId and HIe. In addition, the subfraction P2 obtained byKurokawa & MacLeod[24] was the slowest-migrating component in their SDS/PAGE system, which is typical for rat histone HIb but not for histone Hla[17]. Thus the present study suggests that the subfraction P2 obtained by Kurokawa & MacLeod[24] (our subfraction, p2) in reality consists of histone Hlb.…”

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“…In addition, the subfraction P2 obtained byKurokawa & MacLeod[24] was the slowest-migrating component in their SDS/PAGE system, which is typical for rat histone HIb but not for histone Hla[17]. Thus the present study suggests that the subfraction P2 obtained by Kurokawa & MacLeod[24] (our subfraction, p2) in reality consists of histone Hlb. The genuine histone HI a (our subfraction p3), however, is eluted immediately before histone Hld and was not separated byKurokawa & MacLeod[24].…”

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confidence: 50%

“…The biological results obtained by these different analytical methods cannot readily be compared, however. Thus [24], Karhu et al [I1] and Quesada et al [15] tried to set up a correlation between the HI subfractions separated by h.p.l.c. and the nomenclature systems of Seyedin & Kistler [17] and Lennox et al [16].…”

Section: Introductionmentioning

confidence: 99%

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Separation of rat tissue histone H1 subtypes by reverse-phase h.p.l.c. Identification and assignment to a standard H1 nomenclature

Lindner

Helliger

Puschendorf

1990

Biochemical Journal

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H1 histones from rat liver and rat testis were separated by reverse-phase h.p.l.c. Within 40 min six subfractions (H1(0), H1b, H1a, H1d, H1e + H1c and H1c) and seven subfractions (H1(0), H1b, H1a, H1d, H1e + H1c, H1c and H1t) respectively were isolated by using a linear acetonitrile gradient. Each individual H1 subtype was identified either by comparing the H1 variants (contained in both tissues but in different quantities) or by SDS/PAGE and acetic acid/urea/PAGE. Moreover, all H1 variants were characterized by amino acid analyses. The amino acid compositions of rat histone subfractions H1(0), H1b and H1e were determined for the first time. It was possible to classify unambiguously the H1 subfractions obtained by h.p.l.c. by following the standardized H1 nomenclature for electrophoretic systems recommended by Lennox, Oshima & Cohen [(1982) J. Biol. Chem. 257, 5183-5189]. Incorrect assignments that have been made in various publications are discussed.

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Separation of rat tissue histone H1 subtypes by reverse-phase h.p.l.c. Identification and assignment to a standard H1 nomenclature

Lindner

Helliger

Puschendorf

1990

Biochemical Journal

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“…Applying the chromatographic conditions mentioned before often in combination with short C4 and C8 columns (10 cm), which give even superior results, linker and core histones from a variety of tissues and tumor cells from various species were analyzed by Lindner et al [45,46,73,79,92]. An eluent system similar to that already reported by Certa and von Ehrenstein [80], but in combination with large-pore materials, was utilized by Kurokawa and MacLeod [81] for the separation of rat liver histones. While resolution was satisfying, the presence of sodium perchlorate and phosphate in the eluent prevented it from being volatile, and, thus, suited for online MS detection.…”

Section: Rp-hplcmentioning

confidence: 99%

Analysis of histones, histone variants, and their post‐translationally modified forms

Lindner

2008

Electrophoresis

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For many years, histones were considered passive structural components of eukaryotic chromatin. Meanwhile it has been proven that histones also participate in gene regulation and repression via post-translational modification. The multitude of these post-translational modifications and the existence of numerous histone variants require particular separation strategies for their analysis, a prerequisite for studying biological processes. The most widely utilized techniques for the separation of histones, namely PAGE, HPCE, RP-HPLC, and hydrophilic Interaction LC, are reviewed here. Problems inherent to the analysis of histones owing to their unique physical and chemical properties along with advantages and shortcomings of particular methods are discussed.

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“…HZB, H3, and H4 in approximately equimolar amounts, with only slight contamination by histone H1 and by nonhistone proteins. Further analysis of the proteins in core particles by a high resolution HPLC method [30] indicated that the subtypes of H2A and H3 normally seen in rat liver nuclei 1311 were also found in the core particle preparations (data not shown). In some experiments, the KCI-precipitated chromatosomes were analyzed and found, as expected 1241. to contain histone H1 in addition to the core histones.…”

Section: Preparation Of Core Particlesmentioning

confidence: 99%

Interaction of an ultimate carcinogen, benzo[a]pyrene diol epoxide, with nucleosomal core particles: Apparent lack of protection of DNA by histone proteins

MacLeod

Smith

Lew

1989

Molecular Carcinogenesis

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The binding of chemical carcinogens to nuclear macromolecules, especially to DNA, is thought to be central to the initiation of carcinogenesis. Previous studies of the interactions of one such ultimate carcinogen, benzo[a]pyrene diol epoxide (BPDE-I) with nuclei, chromatin and purified DNA, demonstrated that although some BPDE-I-DNA interactions were altered in chromatin, covalent binding to chromatin DNA at saturating chromatin concentrations was quantitatively the same as binding to purified DNA. We have now extended these studies to include the basic subunit of chromatin, the nucleosomal core particle. Association constants for BPDE-I and a nonreactive analogue were determined by absorbance and fluorescence spectroscopy using either core particles or purified DNA and were found to be lower, by a factor of 30, for core particles. One of the major pathways of interaction of BPDE-I with DNA is the catalysis of BPDE-I hydrolysis by the exocyclic amino group of deoxyguanosine in native DNA. This detoxification reaction is inhibited about 30-fold in core particles compared with DNA, consistent with the hypothesis that intercalation is important in this catalytic reaction. In contrast to these findings, at DNA concentrations that allow maximal binding, similar amounts of BPDE-I are bound covalently to either free DNA or the DNA contained in core particles. This finding suggests that the interaction of DNA with histones to form the subunit structure of chromatin does not significantly protect DNA from damage by this ultimate carcinogen. The pattern of DNA adducts formed with core particle DNA shows a subtle shift toward the pattern seen with denatured DNA.

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Separation of histones by reverse-phase high-performance liquid chromatography: Analysis of the binding of carcinogens to histones

Cited by 25 publications

References 30 publications

Separation of rat tissue histone H1 subtypes by reverse-phase h.p.l.c. Identification and assignment to a standard H1 nomenclature

Separation of rat tissue histone H1 subtypes by reverse-phase h.p.l.c. Identification and assignment to a standard H1 nomenclature

Analysis of histones, histone variants, and their post‐translationally modified forms

Interaction of an ultimate carcinogen, benzo[a]pyrene diol epoxide, with nucleosomal core particles: Apparent lack of protection of DNA by histone proteins

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