Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Purification and spectral cataltic characterization of NADH-cytochrome b reductase
Download
005435.pdf
Date
1989
Author
Güray, Tülin
Metadata
Show full item record
Item Usage Stats
169
views
0
downloads
Cite This
Subject Keywords
Cytochemistry
,
Biochemistry
URI
https://hdl.handle.net/11511/11791
Collections
Graduate School of Natural and Applied Sciences, Thesis
Suggestions
OpenMETU
Core
PURIFICATION OF NADH-CYTOCHROME-B5 REDUCTASE FROM SHEEP LUNG AND ITS ELECTROPHORETIC, SPECTRAL AND SOME OTHER PROPERTIES
Güray, Nülüfer Tülün (Elsevier BV, 1990-01-01)
1. 1. NADH-cytochrome b5 reductase was purified from sheep lung microsomes in the presence of non-ionic and ionic detergents. Emulgen 913 and cholate, respectively. 2. 2. The purification procedure involved the ion-exchange chromatography of the detergent solubilized microsomes on DEAE-cellulose. 3. 3. Further purification and concentration of lung reductase was carried out with a second DEAE-cellulose column followed by the affinity column chromatography of partially purified reductase on 5'-ADP-agarose ...
Purification of glutathione S-transferases and genetic characterization of Zeta isozyme from Pinus brutia, Ten
Öztetik, Elif; İşcan, Mesude; Department of Biochemistry (2005)
Glutathione S-transferases (GST, EC2.5.1.18) are a family of multifunctional, dimeric enzymes that catalyse the nucleophilic attack of the tripeptide glutathione (?-L-glutamyl-L-cysteinyl-L-glycine) on lipophilic compounds with electrophilic centres. The primary function of GSTs is generally considered to be the detoxification of both endogenous and xenobiotic compounds. Cytosolic GSTs have been grouped into eleven distinct classes as: (A); Alpha, (M); Mu, (P); Pi, (S); Sigma, (T); Theta, (Z); Zeta, (F); Ph...
Construction of gay identity among different classes : a case study in Ankara
Ural, Haktan; Beşpınar Akgüner, Fatma Umut; Department of Sociology (2010)
This thesis mainly aims to understand how construction of gay identity differentiates in terms of class inequalities. Regarding the conceptual framework of Deniz Kandiyoti, it inquires in what way class position reshapes the experience of gay sexuality and how gay men of different classes bargain with heteronormative order through different perceptions of homoeroticism and gender identities. In discussing this issue, how gay men identify themselves, how they represent their body, how they interact with and ...
Isolation and immunological characterization of theta class glutathione-s-transferase gstt2-2 from bovine liver
İşgör, Sultan Belgin; Çoruh, Nursen; Department of Biochemistry (2004)
The glutathione-S-transferases (GSTs) (EC.2.5.1.18) are enzymes that participate in cellular detoxification of endogenous as well as foreign electrophilic compounds, function in the cellular detoxification systems and are evolved to protect cells against reactive oxygen metabolites by conjugating the reactive molecules to the nucleophile scavenging tripeptide glutathione (GSH, ?-glu-cys-gly). The GSTs are found in all eukaryotes and prokaryotic systems, in the cytoplasm, on the microsomes, and in the mitoch...
Identification of ligand binding regions of the Saccharomyces cerevisiae alpha-factor pheromone receptor by photoaffinity cross-linking
Son, Çağdaş Devrim; Naider, F; Becker, JM (American Chemical Society (ACS), 2004-10-19)
Analogues of alpha-factor, Saccharomyces cerevisiae tridecapeptide mating pheromone (H-Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr-OH), containing p-benzoylphenylalanine (Bpa), a photoactivatable group, and biotin as a tag, were synthesized using solid-phase methodologies on a p-benzyloxybenzyl alcohol polystyrene resin. Bpa was inserted at positions 1, 3, 5, 8, and 13 of alpha-factor to generate a set of cross-linkable analogues spanning the pheromone. The biological activity (growth arrest assay) ...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
T. Güray, “Purification and spectral cataltic characterization of NADH-cytochrome b reductase,” Ph.D. - Doctoral Program, Middle East Technical University, 1989.