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2 edition of Analysis of a phosphoprotein fraction in rat liver chromatin using an immunological approach. found in the catalog.

Analysis of a phosphoprotein fraction in rat liver chromatin using an immunological approach.

Marvin Joseph Halikowski

Analysis of a phosphoprotein fraction in rat liver chromatin using an immunological approach.

by Marvin Joseph Halikowski

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  • 31 Currently reading

Published .
Written in English


The Physical Object
Pagination132 leaves
Number of Pages132
ID Numbers
Open LibraryOL14744113M

The Content on this Site is presented in a summary fashion, and is intended to be used for educational and entertainment purposes only. It is not intended to be and should not be interpreted as medical advice or a diagnosis of any health or fitness problem, condition or disease; or a recommendation for a specific test, doctor, care provider, procedure, treatment plan, product, or course of action.   Introduction. The rat α 1-acid glycoprotein (AGP) gene is a single copy gene (1) and one of the acute phase protein genes which is expressed in liver cells in the acute phase response (2, 3).Cytokines such as IL-1 and IL-6 activate synthesis of AGP (4, 5).Glucocorticoids also induce AGP (4, 5) and we found that expression of the rat AGP gene was also controlled by thyroid hormone [3,3 Cited by: 3.

Abstract Rat liver chromatin has been fractionated by different solubility in solvents of mᴍ ionic strength in soluble S and insoluble I-chromatin. Histone H1 content is lower in S as compared to I-chromatin. The HMG1/2 nonhistone proteins are observed in S-chromatin and in the nuclear pelleted residue from the chromatin isolation procedure, but no amount can be detected in I-chromatin. Using a reverse genetics approach, Dittmer et al., were able to characterize the Arabidopsis NMCP homologs they named ‘Little Nuclei’ or LINC. In addition to the structural characteristics suggested by sequence homology with NMCP1 and 2 (Table ), T‐DNA insertional double mutants of LINC1 and LINC2 showed significantly smaller nuclei Cited by: 4.

A large compendium of cellular responses to drugs as profiled through proteomic assays of phosphosignaling and histone modifications reveals cellular responses that transcend lineage, discovers unexpected associations between drugs, and recognizes therapeutic hypotheses for treatment of multiple myeloma and acute lymphocytic by:   In adult planarians, the replacement of cells lost to physiological turnover or injury is sustained by the proliferation and differentiation of stem cells known as neoblasts. Neoblast lineage relationships and the molecular changes that take place during differentiation into the appropriate cell types are poorly understood. Here we report the identification and characterization of a cohort of Cited by:


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Analysis of a phosphoprotein fraction in rat liver chromatin using an immunological approach by Marvin Joseph Halikowski Download PDF EPUB FB2

A simple and effective method to purify a phosphoprotein (B2) (Mr 68, pI ) from phenol-soluble non-histone chromatin proteins of rat liver is described.

The purification involved only two steps, CM-cellulose chromatography. Separation of phosphoproteins and protein kinase in rat liver chromatin by phospho-cellulose column chromatography.

The supernatant (see text, 38 mg protein) was applied to a phosphocellulose column ( x 12 cm) equilibrated with M Tris-C1, pHcontaining M NaCl.

Fractions (5 ml each) were collected at a flow rate of ml/ by: Abstract. The concentration of free phosphate groups is measured in rat liver chromatin after DNase II digestion using polylysine titration. The unsheared chromatin completely precipitates at lysine/DNA phosphate ratios of to Author: Matti Vauhkonen, Kari Hemminki.

The nonhistone:DNA ratios in liver of rats fed diet 1 or diet 2 were fold and fold, respectively, larger than control ratios. The histone:DNA ratio remained relatively constant among all three dietary treatments.

Liver nuclei were purified from rats fed each dietary treatment and were solubilized in 9 m urea. The nuclear proteins were analyzed by two-dimensional electrophoresis and Cited by: 4. Analysis of the basal phosphoproteome of rat liver tissue by high-capacity immobilized metal affinity chromatography combined with liquid chromatography-tandem mass spectrometry resulted in the identification of phosphorylated peptides, 75% of which were singly-phosphorylated.

Triplicate analyses highlighted the reproducibility of the by: Subsequently, chromatin fractions containing satellite DNA were isolated from calf thymus (13), African green monkey cells (14), rat liver (7), and mouse liver (15).

Structural Studies on Rat Liver Chromatin There are strong indications that in interphase nuclei the chromatin strands are not freely mobile but are subject to topological by: 1. Acta Biol Acad Sci Hung. ;21(2) Isolation and examination of chromatin fractions from rat liver cells.

Szeszák F, Tomory Z, Szabó : Szeszák F, Tomory Z, Szabó G. Liver weight gain generally corresponded to body weight gain and also reflected hybrid vigor. The protein/DNA ratios of the chromatin from livers of inbred and heterotic hybrid male rats were found to increase with increasing age in growing rats.

Hybrid chromatin had higher protein/DNA ratios throughout the age range by: 3. PROTEIN KINASES AND PHOSPHOPROTEINS IN MEMBRANE FRACTIONS OF RAT LIVER Bengt Jergil, Marianne Sommarin, Thomas Henriksson, and Cecilia Schelin Biochemistry 1, Chemical Centre, Lund, Sweden ABSTRACT Protein kinase and phosphoprotein patterns have been examined in subcellular fractions of rat by: 1.

A protein kinase was purified from liver nuclear chromatin as well as a phosphoprotein fraction. The kinase is able to phosphorylate the phosphoproteins and histone F 2b. Phosphoproteins partly suppressed the histone inhibition of RNA synthesis in the presence of DNA.

Purified protein kinase had no direct effect on it. by: The data presented here suggest that the rat liver chromatin factor is behaving more like an enzyme: it is not active at 0 C and, in the presence of an excess substrate, it is still working after min.

Kinetic analysis are being done to decide if the factor is a stoichiometric reagent or an by: The non-histone nuclear phosphoprotein B2 (Mr 68,; pI ) was found to bind specifically defined fragments of DNA.

With the use of monoclonal IgG2A antibodies prepared against this nuclear. The purified phosphoprotein B2 was shown to be homogeneous by SDS/polyacrylamide-gel electrophoresis. The yield was 2% of total non-histone chromatin proteins. The acidic to basic amino acid ratio of phosphoprotein B2 was less than 1, with high contents of glutamic acid, aspartic acid, arginine, lysine, glycine and by: 3.

Takeda M, Yamamura H, Ohga Y () Phosphoprotein kinases associated with rat liver chromatin. Biochem Biophys Res Commun – PubMed Google Scholar Teng CS, Teng CT, Allfrey VG () Studies of nuclear acidic proteins: Evidence for their phosphorylation, tissue specificity, selective binding to DNA and selective effects on by: Rat liver chromatin has been fractionated into two fractions on the basis of precipitability in standard saline after mild treatment with DNase II.

The major portion of liver chromatin contains little nonhistone protein and is enriched in histones, while a minor portion of such chromatin, with which RNA polymerase is associated, is highly. Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space Article in FEBS Journal (17)   Electrophoretic profiles of acid-extractable proteins from Holtzman rat liver chromatin display four minor and five major histone bands through certain stages of postweaned development but are qualitatively different from the chromatin protein profiles previously reported during postweaned development for the Fisher rat strain and the F × Holtzman heterotic progeny [Tallman, G., et Cited by: 4.

Bradbury, E. and H. Rattle, Simple computer-aided approach for the analysis of the nuclear magnetic resonance spectra of histones fractions F1, F2a1, F2b cleaved halves of F2b and F2b-DNA. Activated transcription from rat liver chromatin by non-histone proteins.

Biochim. Biophys. and L. Hood, Non-histone. Proper liver function is crucial for metabolism control and to clear toxic substances from the bloodstream. Many small-molecule therapeutics accumulate in the liver, negatively impacting liver function and often resulting in hepatotoxicity and cell death.

Several analytical methods are currently utilized to evaluate hepatotoxicity and monitor liver function. To date, none of these methods have Cited by: Phosphorylation analysis by mass spectrometry is generally accomplished by a two-step approach. The phosphoprotein of interest is proteolytically digested, usually with trypsin, and the tryptic peptides are analyzed to determine which are by:.

Chromatin from rat liver citric acid nuclei was extracted 3 times with buffer containing M Tris-HCI (pH ), or M NaCI, and M PMSF at a ratio of 10 ml.Action of DNaseII onrat liver chromatin.

Incuba-tion was at C with 25 ug/ml of DNase II. (A) rat liver chromatinssolublizedbyDNasetreatmentweredeterminedafter centrifugation at30, Xgfor20min(solid circles). Solubilized chromatins were treated with SSC and the percentage of SSC-solublefractions wasdeterminedaftercentrifugation at30, X gfor20min (opencircles).Parafusin, an Exocytic-sensitive Phosphoprotein, Is the Primary Aceeptor for the Glucosyl-phosphotransferase in Paramecium tetraurelia and Rat Liver.