A technique for the determination of protein concentration by neutron activation analysis of silver binding

W. Frasch; J. Larsen; N. Bowlby; I. Apel; J. Jones

doi:10.1007/bf02037279

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Journal of Radioanalytical and Nuclear Chemistry

Volume/Issue:: Volume 112: Issue 1

A technique for the determination of protein concentration by neutron activation analysis of silver binding

Authors:

W. Frasch

W. Frasch The University of Michigan The Division of Biological Sciences 48109 Ann Arbor MI (USA)

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J. Larsen

J. Larsen The University of Michigan The Division of Biological Sciences 48109 Ann Arbor MI (USA)

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N. Bowlby

N. Bowlby The University of Michigan The Division of Biological Sciences 48109 Ann Arbor MI (USA)

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I. Apel

I. Apel The University of Michigan The Division of Biological Sciences 48109 Ann Arbor MI (USA)

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J. Jones

J. Jones The University of Michigan The Phoenix Memorial Laboratory 48109 Ann Arbor MI (USA)

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Pages:: 89–94

Online Publication Date:: 14 Aug 2005

Publication Date:: 17 May 1987

Article Category:: Research Article

DOI:: https://doi.org/10.1007/bf02037279

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Abstract

A method for the quantitative determination of small amounts of protein samples was developed employing neutron activation analysis. Current methods of protein concentration determination are severely limited as a result of differences in the specific characteristics of each protein. Silver binding has been used as a sensitive colorimetric method to indicate the presence of protein. However, silver-protein complexes can have a variety of absorbance spectra unique to each protein, which complicate the analysis. Various amounts of specific proteins were equilibrated in an excess of silver nitrate prior to the reduction of the silver by the addition of NaBH₄, HCHO, and NaOH. The protein-silver complex was rapidly separated from the unbound silver by centrifugation chromatography and the amount of bound silver was determined by INAA. The amount of silver was proportional to the amount of protein present in each sample. When the silver was not reduced prior to removal of the unbound silver by chromatography, only negligible amounts of silver remained bound to the protein. The stoichiometry of bound silver to protein on a molar basis showed relatively small differences for the proteins that were examined. This ratio was found to depend on the conditions of the binding and reduction of the silver. The results suggest that the binding of silver is not specific to any charged or polar groups on these proteins and may, therefore, provide a means of determination of the concentration of protein that has general application for all proteins.

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Journal of Radioanalytical and Nuclear Chemistry

Print ISSN:: 0236-5731

Online ISSN:: 1588-2780

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Journal of Radionalytical and Nuclear Chemistry
Language	English
Size	A4
Year of Foundation	1968
Volumes per Year	1
Issues per Year	12
Founder	Akadémiai Kiadó
Founder's Address	H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher	Akadémiai Kiadó Springer Nature Switzerland AG
Publisher's Address	H-1117 Budapest, Hungary 1516 Budapest, PO Box 245. CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible Publisher	Chief Executive Officer, Akadémiai Kiadó
ISSN	0236-5731 (Print)
ISSN	1588-2780 (Online)