Avidin-peroxid%C3%A1zaMeerrettichperoxidaseHorseradish_peroxidasePeroxidasa_de_r%C3%A1banoPiparjuuriperoksidaasiPeroxydase_de_raifortPeroxidase_de_ravo_picantePeroksydaza_chrzanowa%D0%9F%D0%B5%D1%80%D0%BE%D0%BA%D1%81%D0%B8%D0%B4%D0%B0%D0%B7%D0%B0_%D1%85%D1%80%D0%B5%D0%BD%D0%B0Peroksidaza_renaPeroxidaza_c%E1%BA%A3i_ng%E1%BB%B1aQ413665%E8%BE%A3%E6%A0%B9%E8%BF%87%E6%B0%A7%E5%8C%96%E7%89%A9%E9%85%B6
about
Mechanistic investigations of horseradish peroxidase-catalyzed degradation of single-walled carbon nanotubesDirect measurement of hydrogen peroxide release from rat alveolar macrophages: artifactual effect of horseradish peroxidaseMetabolic activation of phenol by human myeloperoxidase and horseradish peroxidaseNew pteridine substrates for dihydropteridine reductase and horseradish peroxidaseLocalization of the spinal nucleus of accessory nerve in rat: a horseradish peroxidase studyThe structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substratesDifferential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2The catalytic pathway of horseradish peroxidase at high resolutionStructural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycleCrystal structure of horseradish peroxidase C at 2.15 A resolutionStructural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallographyHorseradish peroxidase: a modern view of a classic enzymeThe connections of the mouse olfactory bulb: a study using orthograde and retrograde transport of wheat germ agglutinin conjugated to horseradish peroxidaseInvestigation of the blood-ganglion barrier properties in rat sympathetic ganglia by using lanthanum ion and horseradish peroxidase as tracersA split horseradish peroxidase for the detection of intercellular protein-protein interactions and sensitive visualization of synapsesComparison of horseradish peroxidase and alkaline phosphatase-labelled antibodies in enzyme immunoassaysDivergent projections of physiologically characterized rat ventral cochlear nucleus neurons as shown by intra-axonal injection of horseradish peroxidaseComplexes of horseradish peroxidase with formate, acetate, and carbon monoxideTransneuronal transport of wheatgerm agglutinin conjugated with horseradish peroxidase in the somatosensory system of the rat: a light- and electron-microscopic studyHaem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-->Met mutantInfluence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase.The enzyme horseradish peroxidase is less compressible at higher pressures.Low concentration of silver nanoparticles not only enhances the activity of horseradish peroxidase but alter the structure alsoHow modification of accessible lysines to phenylalanine modulates the structural and functional properties of horseradish peroxidase: a simulation studyThe light side of horseradish peroxidase histochemistry.Afferent neurons in the hypoglossal nerve of the zebra finch (Poephila guttata): localization with horseradish peroxidase.A horseradish peroxidase-light and electron microscopic study of immunoliposomes utilized for intracellular delivery to the rat striatum.Metal coordination influences substrate binding in horseradish peroxidase.The structure of horseradish peroxidase C characterized as a molten globule state after Ca(2+) depletion.Refolding of horseradish peroxidase is enhanced in presence of metal cofactors and ionic liquids.Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase.Presence of endogenous calcium ion in horseradish peroxidase. Elucidation of metal-binding site by substitutions of divalent and lanthanide ions for calcium and use of metal-induced NMR (1H and 113Cd) resonances.Molecular dynamics studies on peroxidases: a structural model for horseradish peroxidase and a substrate adduct.Probing the active site residues in aromatic donor oxidation in horseradish peroxidase: involvement of an arginine and a tyrosine residue in aromatic donor bindingSimultaneous demonstration of horseradish peroxidase and acetylcholinesterase.The basal forebrain projection to the region of the nuclei gemini in the rat; a combined light and electron microscopic study employing horseradish peroxidase, fluorescent tracers and Phaseolus vulgaris-leucoagglutinin.The interaction of cationic liposomes containing entrapped horseradish peroxidase with cells in culture.Vascular permeability to horseradish peroxidase in brainstem lesions of thiamine-deficient rats.Distribution of primary afferent fibres in the cochlear nuclei. A silver and horseradish peroxidase (HRP) study.Distribution of primary cochlear afferents in the bulbar nuclei of the rat: a horseradish peroxidase (HRP) study in parasagittal sections.
P921
Q23910527-728F13FC-3262-4DA5-8061-609345801296Q23917430-88D564B1-5DFD-4358-B31D-529A90E6183EQ23922634-BD8DA3D8-02F3-4F62-9EA1-F54C9FF16C16Q24529192-DFACF46E-187A-4DFF-8ADB-20FFCD965633Q24684149-3F86B9B0-8620-49F5-A692-99415F51A816Q27620499-8D5462DF-60DE-4193-8F30-7E6FE39AC9F0Q27634774-5A82B53B-259A-4BB6-8A77-FA5CB1DB1EA2Q27639029-0D2A3AFC-756B-4983-89DE-A3EAC1EC6A7BQ27639708-C7DA5C38-9B28-498A-87EC-92B0F3F9C096Q27748751-9B8145C2-4C31-4D33-8686-4A1CE5F8D08AQ27758189-102D9A42-A0B1-48B4-AA70-E3F3972D242CQ28241511-DC7E1985-C1B9-42B4-AECD-56D7D737B02AQ28262988-19AF5FEC-8C54-4201-B8EA-C35BBD344A30Q28273201-A4A517BB-F7D3-40DC-B0D5-D5C2C4540C78Q28276002-42598CF5-7B9A-4C3D-B712-37A2E82AFFB2Q28288416-BBF800F7-1993-440E-96ED-2885BDA8A92EQ28293081-011DD66E-35FE-4ACD-8C6D-3AE5953666D3Q28301858-B54B8435-DFA1-4DC3-B75F-173AB7ED5482Q28336918-382CAED7-4246-4B36-8BFF-60FDFEBCD562Q28345500-DAC0297C-31EF-4EF7-8705-D838CFFB7E20Q28365192-AC001026-1656-4495-9B6D-344EDFD6C1B7Q28366872-7BE9F50E-9A8D-48AB-A288-EDFADACB642DQ28481636-BA66B1FD-4706-4199-AF76-B36BAD7FDC7FQ28543737-A2D6AD8D-46A7-4D85-B1F9-AD67E6CCD8D9Q29039344-1C4ACD00-F724-44C4-8339-20DDBD182664Q30011330-04237B12-CEA0-4E58-B806-B60EB88BF802Q30310213-EA7F3FD9-A014-4796-9DAF-7D6BEED3E302Q30327496-8ED79C1E-94BD-433A-985F-D034B914EC4BQ30372171-F28584BC-6EC8-4A19-AEFA-EF9B3DACB165Q30384721-0BEE5F2D-23F7-468E-A09A-FCE7C5DCE512Q30403403-1E8CDD50-E351-4BAC-B0E5-C4A9E9ECE61BQ30406229-3CEF42DD-DA12-4B95-AB05-9D468478AA5AQ30419730-3A33B162-36C7-4A4A-A021-3FC2FABB2CE2Q30423738-6A68D306-C7D5-4F98-9D7E-B80103EEAAEFQ30448768-C7EF53CC-B430-4775-BC8F-ACE2D828067FQ30456558-D19252DA-AC6F-4114-92CB-1DDAED27C87DQ30494595-AE4830EC-4EB3-4F83-BD9B-4CE76EC587D8Q30500264-95D00896-3962-41E9-B636-9042DB5A407CQ30537854-6BA26C95-676C-4C7E-8BDD-D8BB49E0D2C1Q30537856-16E37591-E8A7-45F8-B01C-C8EEE60E1491
P921
description
Protein
@de
chemesch Verbindung
@lb
chemical compound
@en-ca
chemical compound
@en-gb
chemická sloučenina
@cs
chemická zlúčenina
@sk
chemiese verbinding
@af
chemische Verbindung
@de-ch
chemische verbinding
@nl
class of enzymes
@en
name
Avidin-peroxidáza
@cs
Horseradish peroxidase
@en
Meerrettichperoxidase
@de
Peroksidaza rena
@sr
Peroksydaza chrzanowa
@pl
Peroxidasa de rábano
@es
Peroxidase de ravo picante
@gl
Peroxidaza cải ngựa
@vi
Peroxydase de raifort
@fr
Piparjuuriperoksidaasi
@fi
type
label
Avidin-peroxidáza
@cs
Horseradish peroxidase
@en
Meerrettichperoxidase
@de
Peroksidaza rena
@sr
Peroksydaza chrzanowa
@pl
Peroxidasa de rábano
@es
Peroxidase de ravo picante
@gl
Peroxidaza cải ngựa
@vi
Peroxydase de raifort
@fr
Piparjuuriperoksidaasi
@fi
altLabel
Avidin peroxidasa
@cs
Avidin peroxidáza
@cs
Avidin-peroxidasa
@cs
Avidinperoxidasa
@cs
Avidinperoxidáza
@cs
HRP
@nn
Horse Radish Peroxidase
@de
prefLabel
Avidin-peroxidáza
@cs
Horseradish peroxidase
@en
Meerrettichperoxidase
@de
Peroksidaza rena
@sr
Peroksydaza chrzanowa
@pl
Peroxidasa de rábano
@es
Peroxidase de ravo picante
@gl
Peroxidaza cải ngựa
@vi
Peroxydase de raifort
@fr
Piparjuuriperoksidaasi
@fi
P486
P6366
P646
P18
P279
P3073
P3117
DTXSID001010860
P486
P591
P6366
2777676563
P646
/m/02pmj05
P672
D08.811.682.732.512