The oxidation of naphthalene sulfonate dyes by horse radish peroxidase

Lydia Sasson; Michaela Sharabani; Irit Aviram

doi:10.1016/0003-9861(82)90534-3

The oxidation of naphthalene sulfonate dyes by horse radish peroxidase

Lydia Sasson
, Michaela Sharabani
, Irit Aviram^*

^*Corresponding author for this work

Biochemistry Molecular Biology

Tel Aviv University

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10^-12 m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.

Original language	English
Pages (from-to)	529-535
Number of pages	7
Journal	Archives of Biochemistry and Biophysics
Volume	217
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(82)90534-3
State	Published - Sep 1982

Access to Document

10.1016/0003-9861(82)90534-3

Cite this

@article{849b04bf6a4d4d81a150ae7ef0da5a21,

title = "The oxidation of naphthalene sulfonate dyes by horse radish peroxidase",

abstract = "Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10-12 m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.",

author = "Lydia Sasson and Michaela Sharabani and Irit Aviram",

year = "1982",

month = sep,

doi = "10.1016/0003-9861(82)90534-3",

language = "אנגלית",

volume = "217",

pages = "529--535",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - The oxidation of naphthalene sulfonate dyes by horse radish peroxidase

AU - Sasson, Lydia

AU - Sharabani, Michaela

AU - Aviram, Irit

PY - 1982/9

Y1 - 1982/9

N2 - Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10-12 m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.

AB - Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10-12 m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.

UR - https://www.scopus.com/pages/publications/0020359454

U2 - 10.1016/0003-9861(82)90534-3

DO - 10.1016/0003-9861(82)90534-3

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0020359454

SN - 0003-9861

VL - 217

SP - 529

EP - 535

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 2

ER -

The oxidation of naphthalene sulfonate dyes by horse radish peroxidase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this