The determination of specific radioactivity of proteins eluted intact from polyacrylamide gels, utilizing a fluorescamine assay

Laura L. Kilgore; Julie L. Rogers; Bruce W. Patterson; Nancy H. Miller; Waldo R. Fisher

doi:10.1016/0003-2697(85)90335-5

The determination of specific radioactivity of proteins eluted intact from polyacrylamide gels, utilizing a fluorescamine assay

Laura L. Kilgore, Julie L. Rogers, Bruce W. Patterson, Nancy H. Miller, Waldo R. Fisher

Division of Nutritional Science & Obesity Medicine

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

3 Scopus citations

Abstract

The methodology described permits the measurement of the specific radioactivity of diverse proteins resolvable by separatory techniques using cylindrical polyacrylamide gels. Following separation, the proteins are electroeluted; eluted protein is quantitated in the microgram range using a fluorescamine assay, while the major portion of the recovered sample is used for radioactivity measurement. These procedures have been adapted for use in tracer studies of protein metabolism. Their utility in kinetic investigations is demonstrated with data on the time course of changing specific radioactivities of human plasma albumin and apolipoprotein B labeled in vivo with a [³H]leucine tracer.

Original language	English
Pages (from-to)	113-119
Number of pages	7
Journal	Analytical Biochemistry
Volume	145
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(85)90335-5
State	Published - Feb 15 1985

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abstract = "The methodology described permits the measurement of the specific radioactivity of diverse proteins resolvable by separatory techniques using cylindrical polyacrylamide gels. Following separation, the proteins are electroeluted; eluted protein is quantitated in the microgram range using a fluorescamine assay, while the major portion of the recovered sample is used for radioactivity measurement. These procedures have been adapted for use in tracer studies of protein metabolism. Their utility in kinetic investigations is demonstrated with data on the time course of changing specific radioactivities of human plasma albumin and apolipoprotein B labeled in vivo with a [3H]leucine tracer.",

author = "Kilgore, {Laura L.} and Rogers, {Julie L.} and Patterson, {Bruce W.} and Miller, {Nancy H.} and Fisher, {Waldo R.}",

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T1 - The determination of specific radioactivity of proteins eluted intact from polyacrylamide gels, utilizing a fluorescamine assay

AU - Kilgore, Laura L.

AU - Rogers, Julie L.

AU - Patterson, Bruce W.

AU - Miller, Nancy H.

AU - Fisher, Waldo R.

PY - 1985/2/15

Y1 - 1985/2/15

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AB - The methodology described permits the measurement of the specific radioactivity of diverse proteins resolvable by separatory techniques using cylindrical polyacrylamide gels. Following separation, the proteins are electroeluted; eluted protein is quantitated in the microgram range using a fluorescamine assay, while the major portion of the recovered sample is used for radioactivity measurement. These procedures have been adapted for use in tracer studies of protein metabolism. Their utility in kinetic investigations is demonstrated with data on the time course of changing specific radioactivities of human plasma albumin and apolipoprotein B labeled in vivo with a [3H]leucine tracer.

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JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 1

ER -

The determination of specific radioactivity of proteins eluted intact from polyacrylamide gels, utilizing a fluorescamine assay

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