Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking

Paul M. Horowitz; John C Lee; Geri A. Williams; Robert F. Williams; Larry D. Barnes

doi:10.1016/0003-2697(84)90672-9

Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking

Paul M. Horowitz, John C Lee, Geri A. Williams, Robert F. Williams, Larry D. Barnes

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

12 Scopus citations

Abstract

The preparation of acrylamide-agarose gels lacking covalent crosslinking with methylenebis-acrylamide is described. These hybrid gels melt at 85°C and, consequently, allow quantitative analysis of tritium-labeled protein after electrophoresis. Recovery of tritium-labeled ribonucleic acids extracted from hybrid gels is 20 to 25% greater than from standard acrylamide-methylenebisacrylamide gels. Standard curves of electrophoretic mobilities as a function of molecular weights of dissociated proteins and ribonucleic acids are compared for acrylamide-agarose gels and acrylamide-methylenebisacrylamide gels.

Original language	English (US)
Pages (from-to)	333-340
Number of pages	8
Journal	Analytical Biochemistry
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/0003-2697(84)90672-9
State	Published - Dec 1984
Externally published	Yes

Keywords

acrylamide
agarose
gel electrophoresis
nucleic acids
proteins

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0003-2697(84)90672-9

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title = "Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking",

abstract = "The preparation of acrylamide-agarose gels lacking covalent crosslinking with methylenebis-acrylamide is described. These hybrid gels melt at 85°C and, consequently, allow quantitative analysis of tritium-labeled protein after electrophoresis. Recovery of tritium-labeled ribonucleic acids extracted from hybrid gels is 20 to 25% greater than from standard acrylamide-methylenebisacrylamide gels. Standard curves of electrophoretic mobilities as a function of molecular weights of dissociated proteins and ribonucleic acids are compared for acrylamide-agarose gels and acrylamide-methylenebisacrylamide gels.",

keywords = "acrylamide, agarose, gel electrophoresis, nucleic acids, proteins",

author = "Horowitz, {Paul M.} and Lee, {John C} and Williams, {Geri A.} and Williams, {Robert F.} and Barnes, {Larry D.}",

note = "Funding Information: We thank Angela K. Robinson for assistancein iso- lation of tubulin and diadenosine tetraphosphate pyro-phosphohydrolase and Jean Floyd and Connie Mumford for assistance in photolabeling tubulin. Dr. Neal C. Robinson and Dr. Philip Serwer kindly donated “C-methylated proteins and HGT(P) and HEEO agaroses, respectively. This research was supported by National Institutes of Health Grants GM27220 (L.D.B.), GM25 177 (P.M.H.), and GM30665 (R.F.W.), and Robert A. Welch Foundation Grants AQ-723 (P.M.H.), AX-769 (R.F.W.), and AQ-774 (L.D.B.).",

year = "1984",

month = dec,

doi = "10.1016/0003-2697(84)90672-9",

language = "English (US)",

volume = "143",

pages = "333--340",

journal = "Analytical Biochemistry",

issn = "0003-2697",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking

AU - Horowitz, Paul M.

AU - Lee, John C

AU - Williams, Geri A.

AU - Williams, Robert F.

AU - Barnes, Larry D.

N1 - Funding Information: We thank Angela K. Robinson for assistancein iso- lation of tubulin and diadenosine tetraphosphate pyro-phosphohydrolase and Jean Floyd and Connie Mumford for assistance in photolabeling tubulin. Dr. Neal C. Robinson and Dr. Philip Serwer kindly donated “C-methylated proteins and HGT(P) and HEEO agaroses, respectively. This research was supported by National Institutes of Health Grants GM27220 (L.D.B.), GM25 177 (P.M.H.), and GM30665 (R.F.W.), and Robert A. Welch Foundation Grants AQ-723 (P.M.H.), AX-769 (R.F.W.), and AQ-774 (L.D.B.).

PY - 1984/12

Y1 - 1984/12

N2 - The preparation of acrylamide-agarose gels lacking covalent crosslinking with methylenebis-acrylamide is described. These hybrid gels melt at 85°C and, consequently, allow quantitative analysis of tritium-labeled protein after electrophoresis. Recovery of tritium-labeled ribonucleic acids extracted from hybrid gels is 20 to 25% greater than from standard acrylamide-methylenebisacrylamide gels. Standard curves of electrophoretic mobilities as a function of molecular weights of dissociated proteins and ribonucleic acids are compared for acrylamide-agarose gels and acrylamide-methylenebisacrylamide gels.

AB - The preparation of acrylamide-agarose gels lacking covalent crosslinking with methylenebis-acrylamide is described. These hybrid gels melt at 85°C and, consequently, allow quantitative analysis of tritium-labeled protein after electrophoresis. Recovery of tritium-labeled ribonucleic acids extracted from hybrid gels is 20 to 25% greater than from standard acrylamide-methylenebisacrylamide gels. Standard curves of electrophoretic mobilities as a function of molecular weights of dissociated proteins and ribonucleic acids are compared for acrylamide-agarose gels and acrylamide-methylenebisacrylamide gels.

KW - acrylamide

KW - agarose

KW - gel electrophoresis

KW - nucleic acids

KW - proteins

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U2 - 10.1016/0003-2697(84)90672-9

DO - 10.1016/0003-2697(84)90672-9

M3 - Article

C2 - 6085222

AN - SCOPUS:0021704743

SN - 0003-2697

VL - 143

SP - 333

EP - 340

JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 2

ER -

Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking

Abstract

Keywords

ASJC Scopus subject areas

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