Effect of 2,4-dinitrophenol and azide on the latent apyrase activity of the toad embryo.
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2,4-Dinitrophenol↗
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Results for “Azides”
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Progressive inhibition of the catalase-hydrogen peroxide system by acetate, chloride and azide.
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Acetates↗
Synthesis of N-trityl peptides by the Curtius azide method.
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Azides↗
The effect of 2,4-dinitrophenol and sodium azide on anaerobic metabolism of hexoses in Ehrlich ascites tumor cells.
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2,4-Dinitrophenol↗
The oxidase activity of porcine ceruloplasminand its inhibition by azide.
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Animals↗
Investigations on the reaction of azide with sperm whale ferrimyoglobin.
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Animals↗
Effects of 2,4-substituents of deuteroheme upon peroxidase functions. II. Reactions of peroxidases and metmyoglobin with azide, cyanide and fluoride.
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Animals↗
An aryl azide suitable for photoaffinity labeling of amine groups in proteins.
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Amines↗
Inhibition of superoxide dismutases by azide.
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Animals↗
Role of water in protein reactions: binding of azide ion to ferrihemoglobin in water and ethylene glycol mixtures.
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Azides↗
Inhibition of the catecholase and cresolase activity of mushroom tyrosinase by azide.
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Agaricales↗
Azide inhibition of mitochondrial electron transport. I. The aerobic steady state of succinate oxidation.
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Adenine Nucleotides↗
Effects of sodium azide and 2,4-dinitrophenol on phosphorylation reactions and ion fluxes in Saccharomyces cerevisiae.
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Azides↗
The redox states of respiratory-chain components in rat-liver mitochondria. I. Effect of varying substrate concentration and of azide.
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Adenine Nucleotides↗
Biochemical and biophysical studies on cytochrome c oxidase. XI. Reaction with azide.
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Animals↗
Biochemical and biophysical studies on cytochrome c oxidase. XII. Kinetics of azide binding.
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Animals↗
Biochemical and biophysical studies on cytochrome c oxidase. XIX. An EPR study of the photodissociation of carboxycytochrome c oxidase in the presence of azide.
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Animals↗
Localization of regions of the Torpedo californica nicotinic acetylcholine receptor labeled with an aryl azide derivative of phosphatidylserine.
A photoactivatable analog of phosphatidylserine, 125I-labeled 4-azidosalicylic acid-phosphatidylserine (125I-ASA-PS) (Blanton, M. and Wang, H.H. (1990) Biochemistry 29, 1186-1194) was used to label the nicotinic acetylcholine receptor. The photoactivatable group of 125I-ASA-PS is attached directly to the phospholipid head group making it an excellent probe of regions of the AchR structure in contact with the negatively-charged head group of phosphatidylserine. The 'binding domains' were localized by chemically cleaving the labeled receptor with cyanogen bromide (CNBr), separating the generated peptides by reverse-phase HPLC, and N-terminal sequence analysis of radiolabeled material. CNBr fragments containing flanking regions of the transmembrane spanning region M4 as well as within M3 were identified within HPLC separated radiolabeled material. The results suggest a topological arrangement of the transmembrane helices in which the hydrophobic faces of M3 and M4 form the boundary of the receptor complex in contact with the lipid bilayer.
Amino Acid Sequence↗