Zobrazeno 1 - 10
of 358
pro vyhledávání: '"Hemichrome"'
Autor:
Olga Dotsenko, Galyna Taradina
Publikováno v:
Біологічні студії, Vol 18, Iss 4, Pp 3-20 (2024)
Background. In recent years, many publications have highlighted the role of erythrocytes in the pathogenesis of various acute and chronic diseases. Their negative impact is explained by the ability of these cells to generate superoxide anion-radical
Externí odkaz:
https://doaj.org/article/d7cddb97f53c434f892bb465ea3c0f79
Publikováno v:
MethodsX, Vol 7, Iss , Pp 100836- (2020)
Hemoglobin derivatives are often quantified in blood to establish cardio-respiratory status and possible causes of impaired oxygen transport. The derivative known as methemoglobin results from oxidation of hemoglobin and is pathologically relevant be
Externí odkaz:
https://doaj.org/article/651de6690fb24208bad3d9e4607e8f56
Akademický článek
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Publikováno v:
Regulatory Mechanisms in Biosystems. 12:452-458
The early signs of vibration effects on the human body are microcirculation and transcapillary metabolism disorders, accompanied by disruption of the supply to and utilization of oxygen in the tissues and organs. However, there are few experimental s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::291c7dce114be641520865b6bdd8c162
https://doi.org/10.15421/022162
https://doi.org/10.15421/022162
Publikováno v:
Avicenna Journal of Medical Biochemistry, Vol 8, Iss 1, Pp 21-26 (2020)
Background: Hemoglobin (Hb), oxygen, carbon dioxide, and electron transporter of the body, may enter to an oxidation process that can convert oxyhemoglobin (oxyHb) to methemoglobin (metHb) and hemichrome. Surfactants can facilitate oxidation process
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fc2e86b873dc86b0384c151afcb1664
https://doi.org/10.34172/ajmb.2020.03
https://doi.org/10.34172/ajmb.2020.03
Autor:
Mark A. White, William C. Ou, Premila P. Samuel, David A. Case, George N. Phillips, John S. Olson
Publikováno v:
Biophysical Journal. 118:1381-1400
Hemoglobin functions as a tetrameric oxygen transport protein, with each subunit containing a heme cofactor. Its denaturation, either in vivo or in vitro, involves autoxidation to methemoglobin, followed by cofactor loss and globin unfolding. We have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::656330714720253edc7274695ed4519d
https://doi.org/10.1016/j.bpj.2020.01.031
https://doi.org/10.1016/j.bpj.2020.01.031
Autor:
Yoshiaki Sugawara, Mai Yamada, Eriko Ueno, Mai Okazaki, Aya Okamoto, Mariko Miyake, Fusako Fukami, Ai Yano
Publikováno v:
Applied Sciences, Vol 1, Iss 1, Pp 13-55 (2011)
Cellular life is reliant upon rapid and efficient responses to internal and external conditions. The basic molecular events associated with these processes are the structural transitions of the proteins (structural protein allostery) involved. From t
Externí odkaz:
https://doaj.org/article/2f81ddd209054aff9a18ab9b53cc6604
Autor:
Eriko Ueno, Ikumi Ohgushi, Yoko Abe, Yuki Shigemasa, Yuko Hayashi, Yoshiaki Sugawara, Fumio Shimamoto
Publikováno v:
Sensors, Vol 10, Iss 8, Pp 7099-7121 (2010)
Heinz bodies are intraerythrocytic inclusions of hemichrome formed as a result of hemoglobin (Hb) oxidation. They typically develop in aged red cells. Based on the hypothesis that hemichrome formation is an innate characteristic of physiologically no
Externí odkaz:
https://doaj.org/article/4b9e0f8236b1426da9510e85161ab786
Autor:
Donald A. Belcher, Colbert F. Miller, Abraham K. Badu-Tawiah, Paul W. Buehler, Andre F. Palmer, Jin Hyen Baek, Ivan S. Pires, Richard Hickey
Publikováno v:
Biotechnology and Bioengineering. 117:125-145
Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme-binding pockets that can bind heme or other hydrophobic ligands. Purification of apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30aa0cee24cfff8a54ce6a8f84b906cf
https://doi.org/10.1002/bit.27193
https://doi.org/10.1002/bit.27193
Publikováno v:
Electrochemistry Communications, Vol 102, Iss, Pp 89-93 (2019)
A label-free strategy for imaging blood fingermarks (BFMs) on a hydrophobic poly(vinylidene difluoride) (PVDF) membrane has been developed using scanning electrochemical microscopy (SECM) in the surface interrogation (SI) mode. In this approach, hexa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f5c2f58ace378adba01324a78882db4
http://www.sciencedirect.com/science/article/pii/S1388248119300840
http://www.sciencedirect.com/science/article/pii/S1388248119300840