Results 261 to 270 of about 431,758 (295)

Fluorometric scanning of polyacrylamide gels

Analytical Biochemistry, 1969
Abstract A gel scanning technique that measures the quench of N-allyl-DANSA fluorescence by amido schwarz stained protein bands had the potential capability of about fifty times the sensitivity of absorption densitometric techniques. The preparation of the fluorescent polyacrylamide gels was straightforward and their electrophoretic resolving and ...
John N. Aronson, David P. Borris
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Rapid Destaining of Polyacrylamide Gel

Nature, 1966
WITH increasing use of polyacrylamide gel in zone-electrophoresis, the need for rapid removal of excess stain from the gel increases. The conventional destaining of the gel by washing in 5–7 per cent acetic acid may take from one to several days. This is not only inconvenient but also renders this technique unsuitable for the purification of biological
B. Rogerson, L. K. Nagy, N. Tomkuss
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A modified polyacrylamide gel slicer

Analytical Biochemistry, 1971
Abstract The polyacrylamide gel slicer described by Goldberger in 1968 contained two critical parts which are no longer commercially available. Design changes are presented which allow for construction of this device at reduced cost, using readily available parts.
Gerald L. Moore, Cosmo D. Purpura
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Detection of copper on polyacrylamide gels

Analytical Biochemistry, 1978
Abstract A color test for the localization of copper on polyacrylamide gels is described. The test is based upon the quenching of fluorescence of bathocuproine sulfonate by Cu 1+ and is sensitive to 0.1 nmol of free or protein-bound copper. There is no false positive reaction with 10 nmol of hemeprotein, free Fe 3+ , Fe 2+ , Co 2+ , or Mn 2+ .
Walter J. Bruyninckx, H.S. Mason, S. Gutteridge   +2 more
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Isotachophoresis on Polyacrylamide Gel

Separation Science, 1972
Abstract Isotachophoresis, using Ampholine spacer ions, was applied to the fractionation of two multicomponent protein systems (serum and a urinary preparation tract with Hunter Factor activity) using polyacrylamide gel as a supporting medium. These studies were designed to determine whether isotachophoresis could provide higher load capacity than ...
G. Kapadia, M. Cantz, Andreas Chrambach
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Collapse of polyacrylamide gels

Polymer Bulletin, 1980
Ageing of polyacrylamide gels is connected with the formation of charged groups on network chains. The presence of the electrostatic charges is required for the observation of the gel collapse.
J. A. Torkington, Jaroslav Stejskal, M. Gordon   +2 more
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Isoelectric focusing in polyacrylamide gels

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
From many viewpoints, isoelectric focusing (IEF) represents a major advance in methodology for high-resolution separation of proteins and other amphoteric macromolecules. IEF is essentially an equilibrium method for segregating amphoteric molecules by electrophoresis in stable pH gradients according to their isoelectric points (pI).
Pier Giorgio Righetti, James W. Drysdale
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Ultramicrodetection of proteins in polyacrylamide gels

Analytical Biochemistry, 1992
Here we report the development of a highly sensitive procedure to detect proteins within separation matrices which should facilitate the characterization of rare proteins. The procedure is based on photochemical reactions where very low amounts of silver are deposited around proteins and in a series of steps are converted to silver sulfide.
Andrew Wallace, Hans Peter Saluz
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Drying SDS-Polyacrylamide Gels

Cold Spring Harbor Protocols, 2006
INTRODUCTIONThis protocol describes a method for drying SDS-polyacrylamide gels. Gels containing proteins radiolabeled with 35S-labeled amino acids must be dried before autoradiographic images can be obtained. Nonradioactive gels can also be preserved by drying.
Joseph Sambrook, David W. Russell
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ISOELECTRIC FOCUSING IN POLYACRYLAMIDE GELS

Australian Journal of Experimental Biology and Medical Science, 1970
SummaryAn improved technique for isoelcctric focusing of proteins in polyacrylamide gels is described.In studying insulin with the procedure, mercuric chloride in trichloro‐acetic acid was used to fix the protein in the gel.One major and five minor components were demonstrated in ox and pig insulin.
G.G. Dunckley, Lorraine H Percival, HD Purves   +2 more
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