Characterization of proteome alterations in Phanerochaete chrysosporium in response to lead exposure

Download

index.pdf

Date

2011-03-09

Author

Yildirim, Volkan
ÖZCAN, Servet
Becher, Doerte
Buettner, Knut
Hecker, Michael
Özcengiz, Gülay

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

189
views

39
downloads

Background: Total soluble proteome alterations of white rot fungus Phanerochaete chrysosporium in response to different doses (25, 50 and 100 mu M) of Pb (II) were characterized by 2DE in combination with MALDI-TOF-MS.

Subject Keywords

Biochemistry, Molecular Biology

URI

https://hdl.handle.net/11511/42462

Journal

PROTEOME SCIENCE

DOI

https://doi.org/10.1186/1477-5956-9-12

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

The effect of cysteine-43 mutation on thermostability and kinetic properties of citrate synthase from Thermoplasma acidophilum Kocabıyık, Semra; Russel, RJM; Danson, MJ; Hough, DW (Elsevier BV, 1996-07-05) In this study, we have substituted serine-43 by cysteine in the recombinant citrate synthase from a moderately thermophilic Archaeon Thermoplasma acidophilum, for site-specific attachment of labels and have investigated the effects of this mutation on the biochemical properties and thermal stability of the enzyme. Both wild-type and the mutant enzymes were purified to homogenity using affinity chromatography on Matrex Gel Red A. The mutant Thermoplasma citrate synthase is very similar to wild-type citrate s...
PURIFICATION AND CHARACTERIZATION OF 2 FORMS OF SOLUBLE NADH CYTOCHROME-B5 REDUCTASES FROM HUMAN ERYTHROCYTES ARINC, E; Güray, Nülüfer Tülün; SAPLAKOGLU, U; Adalı, Orhan (Elsevier BV, 1992-01-01) 1. Two forms of soluble NADH cytochrome b5 reductase were purified from human erythrocytes. Two distinct fractions both having the NADH cytochrome b5 reductase activity eluted from the second DEAE-cellulose column were further purified by ultrafiltration and 5'-ADP-agarose affinity chromatography.
Investigating the anticarcinogenic role of salix aegyptiaca l. in colorectal carcinoma Enayat, Shabnam; Banerjee, Sreeparna; Department of Biology (2009) In this study, extracts from bark, leaves and catkins of Salix aegyptiaca L. were investigated for their antioxidant content by 2,2-diphenyl-2-picrylhydrazyl hydrate (DPPH) free radical quenching assay, total phenolic and total flavonoid assays. The highest antioxidant activity (19 ug/ml IC50 for inhibition of DPPH radical activity), total phenolic content (212 mg gallic acid equivalents/g of dried extract) and total flavonoid (479 mg catechin equivalents/g of dried extract) was observed in the ethanolic ex...
Production, purification and characterization of chitosanase from Penicillium spinulosum Ak, O; Bakir, U; Güray, Nülüfer Tülün (1998-11-01) A chitosan degrading fungus which had been isolated in our laboratory and identified as Penicillium spinulosum by the International Mycological Institute (England), was used for the production of chitosanase in a salt medium containing Rhizopus cell walls as the sole carbon source. Although chitosanase was produced under all the conditions tested about 1 % cell wall concentration maximized enzyme production. The enzyme was purified 50 fold by using ammonium sulfate precipitation and ion-exchange chromatogra...
Isolation and characterization of the K5-type yeast killer protein and its homology with an exo-beta-1,3-glucanase Izgu, F; Altinbay, D (Informa UK Limited, 2004-03-01) K5-type yeast killer protein in the culture supernatant of Pichia anomala NCYC 434 cells was concentrated by ultrafiltration and purified to homogenity by ion-exchange chromatography with a POROS HQ/M column followed by gel filtration with a TSK G2000SW column. The protein migrated as a single band on discontinous gradient SDS-PAGE and had a molecular mass of 49000 Da. The pI value of the K5-type killer protein was measured at pH 3.7 by high voltage vertical gel electrofocusing. The result of an enzyme immu...

Citation Formats

V. Yildirim, S. ÖZCAN, D. Becher, K. Buettner, M. Hecker, and G. Özcengiz, “Characterization of proteome alterations in Phanerochaete chrysosporium in response to lead exposure,” PROTEOME SCIENCE, pp. 0–0, 2011, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/42462.