Horseradish Peroxidase-Catalyzed Crosslinking of Fibrin Microthread Scaffolds
نویسندگان
چکیده
منابع مشابه
Horseradish Peroxidase-catalyzed Two-electron Oxidations
The atypical two-electron oxidation of thioanisole and its p-methyl, p-methoxy, and p-nitro analogues by horseradish peroxidase, contrary to earlier reports, stereoselectively produces the (8) sulfoxides in 6070% enantiomeric excess. Horseradish peroxidase reconstituted with 6-meso-ethylheme has little peroxidase (guaiacol oxidizing) activity, as previously reported, but exhibits increased sulf...
متن کاملBiomimetic Synthesis of Resveratrol Trimers Catalyzed by Horseradish Peroxidase.
Biotransformation of trans-resveratrol and synthetic (±)-ε-viniferin in aqueous acetone using horseradish peroxidase and hydrogen peroxide as oxidants resulted in the isolation of two new resveratrol trimers (3 and 4), one new resveratrol derivative (5) with a dihydrobenzofuran skeleton, together with two known stilbene trimers (6 and 7), and six known stilbene dimers (8-13). Their structures a...
متن کاملCharacterization of the N-demethylation reactions catalyzed by horseradish peroxidase.
The hydroperoxide-supported N-demethylation reactions catalyzed by horseradish peroxidase have been characterized in detail. The ethyl hydroperoxide-supported N-demethylation of N,N-dimethylaniline by horseradish peroxidase resulted in the formation of equimolar amounts of N-methylaniline and formaldehyde with no other products detectable by high performance liquid chromatography analysis of th...
متن کاملCharacterization of the N-Demethylation Reactions Catalyzed by Horseradish Peroxidase*
The hydroperoxide-supported N-demethylation reactions catalyzed by horseradish peroxidase have been characterized in detail. The ethyl hydroperoxide-supported N-demethylation of N,N-dimethylaniline by horseradish peroxidase resulted in the formation of equimolar amounts of N-methylaniline and formaldehyde with no other products detectable by high performance liquid chromatography analysis of th...
متن کاملIdentification of acetaminophen polymerization products catalyzed by horseradish peroxidase.
Horseradish peroxidase catalyzed the H2O2-dependent oxidation and polymerization of acetaminophen. Six acetaminophen polymers were isolated from horseradish peroxidase reaction mixtures by semipreparative high pressure liquid chromatography. Chemical structures were determined by a combination of electron impact and chemical ionization mass spectrometry and 500-MHz proton magnetic resonance spe...
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ژورنال
عنوان ژورنال: Tissue Engineering Part C: Methods
سال: 2020
ISSN: 1937-3384,1937-3392
DOI: 10.1089/ten.tec.2020.0083