Ueber die basischen Stoffe des Zellkerns.

Kossel, Albrecht

doi:10.1515/bchm2.1897.22.2.176

Cited by 70 publications

(6 citation statements)

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“…The protocols described here are an optimization and extension of previous histone extraction protocols progressively improved over more than 130 years (Kossel, 1884; Shechter, Dormann, Allis, & Hake, 2007). We describe two protocols that have been streamlined and optimized for three different starting tissue culture cell amounts.…”

Section: Introductionmentioning

confidence: 99%

Expeditious Extraction of Histones from Limited Cells or Tissue Samples and Quantitative Top‐Down Proteomic Analysis

2021

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Histones are the primary protein component of chromatin and are involved in virtually all DNA‐templated processes. Histones are abundantly post‐translationally modified by a variety of chromatin‐modifying machinery. These post‐translational modifications (PTMs) are recognized by a range of “reader” proteins, which recruit additional proteins to specific locations on chromatin and impart precise and powerful effects on gene regulation. Each PTM typically exerts a positive or negative effect on transcription, and recent studies have shown that histone PTMs function in a combinatorial histone code: that is, histone PTMs function in combination to exert precise DNA‐templated regulation. Thus, there is a need to identify and understand proteoforms, or unambiguously defined single protein molecules with all combinations of modifications. Top‐down proteomics is currently the only viable approach for identifying and quantitating histone proteoforms, and mass spectrometry instruments have become sufficiently powerful to perform these quantitative analyses in a robust and high‐throughput fashion. These recent innovations have enabled new experimental directions in chromatin research but have also introduced temporal and other constraints. This has led us to develop the protocols described here, which increase throughput, reduce sample requirements, and maintain robust quantitation. Although originally designed for high‐throughput quantitative top‐down proteomics, the protocols described here are useful for a wide range of chromatin biology applications. Starting with small amounts of cells or tissue, we describe two basic protocols for exceptionally rapid and efficient nuclei isolation, acid extraction of histones, and high‐performance liquid chromatography fractionation of histones into histone families. We additionally describe the quantitative top‐down proteomic analysis of histone H4 proteoforms. © 2021 Wiley Periodicals LLC. Basic Protocol 1: Nuclei isolation and acid extraction of histones from mammalian cells in culture/tissues Basic Protocol 2: HPLC fractionation of histones and histone H4 HPLC‐MS/MS Support Protocol: Preparation of intact H3 histone tails by Glu‐C digestion

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Section: Introductionmentioning

confidence: 99%

Expeditious Extraction of Histones from Limited Cells or Tissue Samples and Quantitative Top‐Down Proteomic Analysis

2021

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“…In some cases, these interactions may also cause liquid-liquid phase separation called complex coacervation. The studies of these interactions date back to 1896, when Kossel reported the first observations of precipitation of egg albumin with addition of oppositely charged protamine [78]. In 1920-1930, Bungenberg de Jong et al [79,80] published several studies on the interactions between gelatin and gum arabic and observed liquid-liquid phase separation and formation of complex coacervates.…”

Section: Figure 3 Schematic Representation Of Formation Of Inter-mmc ...mentioning

confidence: 99%

Interpolymer Complexes of Synthetic, Natural and Semi-Natural Polyampholytes: A Review

Bekturov¹,

Moustafine²,

Kudaibergenov³

et al. 2022

Bull. of the Kar. Univ. "Chem". Ser.

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This review is focused on synthetic, natural and semi-natural polyampholytes and their ability to form interpolymer complexes with other polyelectrolytes and non-ionic polymers. It provides definition, classification and overview of physicochemical properties of polyampholytes. The conformation and phase behaviour of intrinsically disordered proteins and semi-natural polyampholytes derived from aminoacids is discussed. The ability of synthetic, natural and semi-natural polyampholytes to form interpolymer complexes with water-soluble polymers is considered. Most of the research in this area is focused on interpolyelectrolyte complexes of polyampholytes with oppositely charged polyelectrolytes; however, there are also studies demonstrating the formation of hydrogen-bonded complexes. The nature of the complexation is often affected by solution pH and also isoelectric point of polyampholytes. The complexation between polyampholytes and other polymers may lead to formation of colloidal dispersions (nano- and microparticles), liquid-liquid phase separation (called complex coacervation), fully soluble polycomplexes or physically cross-linked gels. A substantial body of studies in this area were focused on the complexes formed by proteins. Application of interpolymer complexes formed by polyampholytes in biotechnology, medicine, encapsulation technologies, separation science, biocatalysis, food science and pharmaceutics is discussed.

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“…The discovery of phase separation of proteins and nucleic acids can perhaps be credited to Albert Kossel, who noted that solutions of proteins can separate into layers: a depleted phase and an enriched phase (59)(60)(61). Although we are only beginning to unravel the multidimensional functional consequences of phase separation, the concept of phase separation as the organizing principle of the cellular interior has existed since the late 1800s (Fig.…”

Section: History Of the Biological Llps Conceptmentioning

confidence: 99%