A sensitive gel filtration method for determination of protein sulfhydryl groups with 14C-chloromercuribenzoate

V. Gene Erwin; Peter L. Pedersen

doi:10.1016/0003-2697(68)90126-7

A sensitive gel filtration method for determination of protein sulfhydryl groups with ¹⁴C-chloromercuribenzoate

V. Gene Erwin, Peter L. Pedersen

School of Medicine

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

20 Scopus citations

Abstract

A gel filtration method employing ¹⁴C-chloromercuribenzoic acid is described for the quantitative determination of sulfhydryl groups in microgram quantities of protein. The method has been applied to several native proteins, hemoglobin, monoamine oxidase, and yeast cytochrome c. In all cases values in close agreement with known literature values were obtained. Horse heart cytochrome c and lysozyme, which have no sulfhydryl groups, did not bind the mercurial reagent. Modifications of the method are described for determining the sulfhydryl content of denatured proteins in the presence of sodium lauryl sulfate. The precision of the method was found to be compatible with known methods for determining the sulfhydryl composition of proteins.

Original language	English (US)
Pages (from-to)	477-485
Number of pages	9
Journal	Analytical biochemistry
Volume	25
Issue number	C
DOIs	https://doi.org/10.1016/0003-2697(68)90126-7
State	Published - 1968

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0003-2697(68)90126-7

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title = "A sensitive gel filtration method for determination of protein sulfhydryl groups with 14C-chloromercuribenzoate",

abstract = "A gel filtration method employing 14C-chloromercuribenzoic acid is described for the quantitative determination of sulfhydryl groups in microgram quantities of protein. The method has been applied to several native proteins, hemoglobin, monoamine oxidase, and yeast cytochrome c. In all cases values in close agreement with known literature values were obtained. Horse heart cytochrome c and lysozyme, which have no sulfhydryl groups, did not bind the mercurial reagent. Modifications of the method are described for determining the sulfhydryl content of denatured proteins in the presence of sodium lauryl sulfate. The precision of the method was found to be compatible with known methods for determining the sulfhydryl composition of proteins.",

author = "Erwin, {V. Gene} and Pedersen, {Peter L.}",

note = "Funding Information: The authors wish to thank Dr. Leslie Hellerman and Dr. A. L. Lehninger for their interest in this work and for a number of useful suggestions prior to publication. Grateful acknowledgment is made to Mrs. JoAnn Hullihen for her technical assistance. This research was supported by grants from the National Institutes Health and the National Science Foundation.",

year = "1968",

doi = "10.1016/0003-2697(68)90126-7",

language = "English (US)",

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pages = "477--485",

journal = "Analytical biochemistry",

issn = "0003-2697",

publisher = "Academic Press Inc.",

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TY - JOUR

T1 - A sensitive gel filtration method for determination of protein sulfhydryl groups with 14C-chloromercuribenzoate

AU - Erwin, V. Gene

AU - Pedersen, Peter L.

N1 - Funding Information: The authors wish to thank Dr. Leslie Hellerman and Dr. A. L. Lehninger for their interest in this work and for a number of useful suggestions prior to publication. Grateful acknowledgment is made to Mrs. JoAnn Hullihen for her technical assistance. This research was supported by grants from the National Institutes Health and the National Science Foundation.

PY - 1968

Y1 - 1968

N2 - A gel filtration method employing 14C-chloromercuribenzoic acid is described for the quantitative determination of sulfhydryl groups in microgram quantities of protein. The method has been applied to several native proteins, hemoglobin, monoamine oxidase, and yeast cytochrome c. In all cases values in close agreement with known literature values were obtained. Horse heart cytochrome c and lysozyme, which have no sulfhydryl groups, did not bind the mercurial reagent. Modifications of the method are described for determining the sulfhydryl content of denatured proteins in the presence of sodium lauryl sulfate. The precision of the method was found to be compatible with known methods for determining the sulfhydryl composition of proteins.

AB - A gel filtration method employing 14C-chloromercuribenzoic acid is described for the quantitative determination of sulfhydryl groups in microgram quantities of protein. The method has been applied to several native proteins, hemoglobin, monoamine oxidase, and yeast cytochrome c. In all cases values in close agreement with known literature values were obtained. Horse heart cytochrome c and lysozyme, which have no sulfhydryl groups, did not bind the mercurial reagent. Modifications of the method are described for determining the sulfhydryl content of denatured proteins in the presence of sodium lauryl sulfate. The precision of the method was found to be compatible with known methods for determining the sulfhydryl composition of proteins.

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SN - 0003-2697

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JO - Analytical biochemistry

JF - Analytical biochemistry

IS - C

ER -

A sensitive gel filtration method for determination of protein sulfhydryl groups with ¹⁴C-chloromercuribenzoate

Abstract

ASJC Scopus subject areas

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