DSpace Community:http://hdl.handle.net/20.500.12323/40752024-03-29T12:12:11Z2024-03-29T12:12:11ZOn the solution of conformable fractional heat conduction equationAllahverdiev, Bilender P.Tuna, HüseyinYalçınkaya, Yükselhttp://hdl.handle.net/20.500.12323/74072024-03-27T07:58:50Z2023-01-01T00:00:00ZTitle: On the solution of conformable fractional heat conduction equation
Authors: Allahverdiev, Bilender P.; Tuna, Hüseyin; Yalçınkaya, Yüksel
Abstract: In this article, we study a conformable fractional heat conduction equation. Applying the method of separation variables to this problem, we get a conformable fractional Sturm–Liouville eigenvalue problem. Later, we prove the existence of a countably infinite set of eigenvalues and eigenfunctions. Finally, we establish uniformly convergent expansions in the eigenfunctions.2023-01-01T00:00:00ZAzerbaycan’da Rus Kilisesi ve Rusçuluk Faaliyetleri (1828-1905)Nusretoğlu, Telmanhttp://hdl.handle.net/20.500.12323/74062024-03-19T10:33:06Z2017-01-01T00:00:00ZTitle: Azerbaycan’da Rus Kilisesi ve Rusçuluk Faaliyetleri (1828-1905)
Authors: Nusretoğlu, Telman2017-01-01T00:00:00ZCeruloplasmin Is an Endogenous Inhibitor of MyeloperoxidaseChapman, Anna L. P.Mocatta, Tessa J.Shiva, SrutiSeidel, AntoniaChen, BrianKhalilova, IradaPaumann-Page, Martina E.Jameson, Guy N. L.Winterbourn, Christine C.Kettle, Anthony J.http://hdl.handle.net/20.500.12323/74052024-03-18T10:46:56Z2013-01-10T00:00:00ZTitle: Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase
Authors: Chapman, Anna L. P.; Mocatta, Tessa J.; Shiva, Sruti; Seidel, Antonia; Chen, Brian; Khalilova, Irada; Paumann-Page, Martina E.; Jameson, Guy N. L.; Winterbourn, Christine C.; Kettle, Anthony J.
Abstract: Myeloperoxidase is a neutrophil enzyme that promotes oxidative stress in numerous inflammatory pathologies. It uses hydrogen peroxide to catalyze the production of strong oxidants including chlorine bleach and free radicals. A physiological defense against the inappropriate action of this enzyme has yet to be identified. We found that myeloperoxidase oxidized 75% of the ascorbate in plasma from ceruloplasmin knock-out mice, but there was no significant loss in plasma from wild type animals. When myeloperoxidase was added to human plasma it became bound to other proteins and was reversibly inhibited. Ceruloplasmin was the predominant protein associated with myeloperoxidase. When the purified proteins were mixed, they became strongly but reversibly associated. Ceruloplasmin was a potent inhibitor of purified myeloperoxidase, inhibiting production of hypochlorous acid by 50% at 25 nm. Ceruloplasmin rapidly reduced Compound I, the Fe(V) redox intermediate of myeloperoxidase, to Compound II, which has Fe(IV) in its heme prosthetic groups. It also prevented the fast reduction of Compound II by tyrosine. In the presence of chloride and hydrogen peroxide, ceruloplasmin converted myeloperoxidase to Compound II and slowed its conversion back to the ferric enzyme. Collectively, our results indicate that ceruloplasmin inhibits myeloperoxidase by reducing Compound I and then trapping the enzyme as inactive Compound II. We propose that ceruloplasmin should provide a protective shield against inadvertent oxidant production by myeloperoxidase during inflammation.2013-01-10T00:00:00ZFractional Dirac Systems with Mittag–Leffler KernelAllahverdiev, Bilender P.Tuna, Hüseyinhttp://hdl.handle.net/20.500.12323/73952024-03-13T06:24:04Z2024-01-01T00:00:00ZTitle: Fractional Dirac Systems with Mittag–Leffler Kernel
Authors: Allahverdiev, Bilender P.; Tuna, Hüseyin
Abstract: In this paper, we study some fractional Dirac-type systems with
the Mittag–Leffler kernel. We extend the basic spectral properties of the ordinary
Dirac system to the Dirac-type systems with the Mittag–Leffler kernel.
First, this problem was handled in a continuous form. The self-adjointness
of the operator produced by this system, the reality of its eigenvalues, and
the orthogonality of the eigenfunctions have been investigated. Later, similar
results were obtained by considering the discrete state.2024-01-01T00:00:00Z