a highly porous sodium dodecyl sulfate-polyacrylamide gel

a highly porous sodium dodecyl sulfate-polyacrylamide gel

A Highly Porous Sodium Dodecyl Sulfate-Polyacrylamide Gel

Abstract. The major contributions to the development of protein separation by gel electrophoresis were the introduction of polyacrylamide gels (Raymond and Weintraub, 1959) and of discontinuous buffer systems (Davis, 1964; Ornstein, 1964), the use of the powerful detergent sodium dodecyl sulfate (SDS) to solubilize protein complexes prior to electrophoresis (Summers et al., 1965), and the

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a discontinuous and highly porous sodium dodecyl sulfate

A discontinuous and highly porous sodium dodecyl sulfate

A highly porous and efficient discontinuous sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis system is described. The slab gel consists of two porous layers of acrylamide of the following composition: 4% acrylamide, 0.04% bisacrylamide for the stacking gel, and 10% acrylamide, 0.1% bisacrylamide for the separating gel, both layers having different buffers.

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modification of a discontinuous and highly porous sodium

Modification of a discontinuous and highly porous sodium

A highly porous and efficient discontinuous sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis system was recently described by J. P. Doucet and J. M. Trifaró [1988) Anal. Biochem. 168, 265-271).

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modification of a discontinuous and highly porous sodium

Modification of a discontinuous and highly porous sodium

A highly porous and efficient discontinuous sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis system was recently described by J. P. Doucet and J. M. Trifaró ((1988) Anal. Biochem. 168, 265–271). The system was developed to separate with high and broad resolution the components from large volume samples after an overnight

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modification of a discontinuous and highly porous sodium

Modification of a discontinuous and highly porous sodium

A highly porous and efficient discontinuous sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis system was recently described by J. P. Doucet and J. M. Trifaró [1988) Anal. Biochem. 168, 265-271). The system was developed to separate with high and broad resolution the components from large volume samples after an overnight electrophoresis. This system was found to have many

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peptide mapping by cnbr fragmentation using a sodium dodecyl

Peptide mapping by CNBr fragmentation using a sodium dodecyl

This has been achieved by combining the advantages of the highly porous SDS'-polyacrylamide slab gel system of Doucet 'Abbreviations used: SDS, sodium dodecyl sulfate; PK, pyruvate kinase; FPLC, fast protein liquid chromatography. and Trifaro (8) with those of vertical polyacrylamide minigel electrophoresis. MATERIALS AND METHODS Materials.

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purification of leucoplast pyruvate kinase from developing

Purification of Leucoplast Pyruvate Kinase from Developing

Doucet JP, Trifaró JM. A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution. Anal Biochem. 1988 Feb 1; 168 (2):265–271. Ibsen KH. Interrelationships and functions of the pyruvate kinase isozymes and their variant forms: a review. Cancer Res. 1977 Feb; 37 (2):341–353.

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purification and molecular and immunological characterization

Purification and Molecular and Immunological Characterization

Doucet JP, Trifaró JM. A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution. Anal Biochem. 1988 Feb 1; 168 (2):265–271. Elrifi IR, Turpin DH. Nitrate and Ammonium Induced Photosynthetic Suppression in N-Limited Selenastrum minutum. Plant Physiol. 1986 May; 81 (1):273–279.

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purification of leucoplast pyruvate kinase from developing

Purification of Leucoplast Pyruvate Kinase from Developing

Doucet JP, Trifaró JM. A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution. Anal Biochem. 1988 Feb 1; 168 (2):265–271. Ibsen KH. Interrelationships and functions of the pyruvate kinase isozymes and their variant forms: a review. Cancer Res. 1977 Feb; 37 (2):341–353.

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chemical modification of ethyl cellulose-based highly porous

Chemical Modification of Ethyl Cellulose-Based Highly Porous

The chemical modification of developed ethyl cellulose-based membrane was carried out to make it suitable for bioseparation. The different reagents were used for the modification of membrane to couple protein A (PA) to study the purification of immunoglobulin G (IgG) from blood.

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peptide mapping by cnbr fragmentation using a sodium dodecyl

Peptide mapping by CNBr fragmentation using a sodium dodecyl

Modification of a discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide gel system for minigel electrophoresis. Doucet JP, Murphy BJ, Tuana BS. Anal Biochem, 190(2):209-211, 01 Nov 1990 Cited by: 37 articles | PMID: 2291467

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[sodium dodecyl sulfate-polyacrylamide gel electrophoresis

[Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

[Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) Objectives: Gel Electrophoresis: Electrophoresis is the movement of molecules by an electric current. Nucleic acid moves from a negative to a positive pole and when DNA is applied to a macromolecular cage or gel such as agarose or polyacrylamide, its migration under the

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sodium dodecyl sulphate polyacrylamide gel electrophoresis

Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis

Sodium dodecyl sulphate (SDS) is an anionic detergent which denatures proteins by "wrapping around" the polypeptide backbone - and SDS binds to proteins fairly specifically in a mass ratio of 1.4:1. In so doing, SDS confers a negative charge to the polypeptide in proportion to its length - ie: the denatured polypeptides become " rods" of

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how sds-page works: 7 key points every scientist should know

How SDS-PAGE Works: 7 Key Points Every Scientist Should Know

SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) is commonly used in the lab for the separation of proteins based on their molecular weight. It’s one of those techniques that is commonly used but not frequently fully understood. So let’s try and fix that by explaining just how SDS-PAGE works.

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sodium dodecyl sulfate polyacrylamide gel electrophoresis

Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), also called the Laemmli system, is commonly used to separate proteins (Gallagher, 2008c). During electrophoresis, SDS plays a role in denaturing proteins and producing a uniform negative charge to enable the proteins to migrate at speeds solely dependent on their molecular

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characteristics of arterial myosin in experimental renal

Characteristics of arterial myosin in experimental renal

on a highly porous sodium dodecyl sulfate-polyacrylamide gel. This protein band cross-reacted with antibody against nonmuscle myosin but not with smooth muscle myosin antibody. The 20- and 17-kd light chains of myosin isolated from normotensive and hypertensive dogs gave similar results on isoelectric focusing.

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purification and molecular and immunological characterization

Purification and Molecular and Immunological Characterization

Doucet JP, Trifaró JM. A discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide slab gel system of high resolution. Anal Biochem. 1988 Feb 1; 168 (2):265–271. Elrifi IR, Turpin DH. Nitrate and Ammonium Induced Photosynthetic Suppression in N-Limited Selenastrum minutum. Plant Physiol. 1986 May; 81 (1):273–279.

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an exponential gradient marker for use with minigel

An exponential gradient marker for use with minigel

Modification of a discontinuous and highly porous sodium dodecyl sulfate-polyacrylamide gel system for minigel electrophoresis. Doucet JP, Murphy BJ, Tuana BS. Anal Biochem, 190(2):209-211, 01 Nov 1990 Cited by: 39 articles | PMID: 2291467

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how sds-page works: 7 key points every scientist should know

How SDS-PAGE Works: 7 Key Points Every Scientist Should Know

SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) is commonly used in the lab for the separation of proteins based on their molecular weight. It’s one of those techniques that is commonly used but not frequently fully understood. So let’s try and fix that by explaining just how SDS-PAGE works.

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what is the use of following in sds-page: sds and beta

What is the use of following in SDS-PAGE: SDS and beta

Polyacrylamide Gel Electrophoresis (PAGE) using Sodium dodecyl sulfate as a detergent. Its polar and nonpolar regions denatures proteins so they unfold. This way they can pass through the gel and the distance traveled is compared to protein standa

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characterization of sodium dodecyl sulfate-stable

Characterization of sodium dodecyl sulfate-stable

Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis has shown wide applicability in the characterization of proteins (2, 9, 11). One application is in bacteriolytic enzyme detection using activity gels.

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‘laterally aggregated’ polyacrylamide gels for

‘Laterally aggregated’ polyacrylamide gels for

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.

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chapter 3: investigating proteins – chemistry

Chapter 3: Investigating Proteins – Chemistry

A detergent such as sodium dodecyl sulfate (SDS) can be used to dissolve cell membranes and keep membrane proteins in solution during purification; however, because SDS causes denaturation, milder detergents such as Triton X-100 or CHAPS can be used to retain the protein’s native conformation during complete purification. Figure 3.2 Dialysis.

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