Gel State Chemiluminescence: An Artificial Electron Transport System

Autor:	Johnathan L. Kiel, David N. Erwin, David M. Simmons
Rok vydání:	1988
Předmět:	Flavin adenine dinucleotide Hemeprotein NADPH oxidase biology food and beverages Cytochrome b559 Flavoprotein Horseradish peroxidase chemistry.chemical_compound chemistry Biochemistry biology.protein Glucose oxidase Peroxidase
Zdroj:	Oxygen Radicals in Biology and Medicine ISBN: 9781468455700
DOI:	10.1007/978-1-4684-5568-7_41
Popis:	Crosslinked glucose oxidase (GO) and horseradish peroxidase (HRP) can mimic macrophage oxidative function in vivo in respect to tumor cells as targets.1–3 Both the flavoprotein of NADPH oxidase of macrophages and GO contain flavin adenine dinucleotide as their prosthetic group. HRP has a noncovalently bound hematoporphyrin IX prosthetic group as does the cytochrome b559 (green hemoprotein) of NADPH oxidase. Therefore, we anticipated a similarity in biochemical mechanism of action and chemi-luminescence (CL) between the semi-synthetic crosslinked GO and HRP and the macrophage NADPH oxidase.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9a006bfe877957a8d01b44cafd347380 https://doi.org/10.1007/978-1-4684-5568-7_41 Zobrazit plný text záznamu