scholarly journals Native SDS-PAGE: high resolution electrophoretic separation of proteins with retention of native properties including bound metal ions

Metallomics ◽  
2014 ◽  
Vol 6 (5) ◽  
pp. 1068-1078 ◽  
Author(s):  
Andrew B. Nowakowski ◽  
William J. Wobig ◽  
David H. Petering
Keyword(s):  
High Resolution ◽  
Metal Ions ◽  
Gel Electrophoresis ◽  
Soluble Proteins ◽  
Electrophoretic Separation ◽  
Enzymatic Function ◽  
Sds Page ◽  
Metal Cofactors ◽  
Separation Of Proteins

Systematical modifications of traditional gel electrophoresis have yielded a method to separate soluble proteins with high resolution while retaining metal cofactors and enzymatic function.

Enhanced electrophoretic separation of proteins by tethered SiO2 nanoparticles in an SDS-polyacrylamide gel network

The Analyst ◽  
2020 ◽  
Vol 145 (2) ◽  
pp. 415-423 ◽  
Author(s):  
Sayyed Hashem Sajjadi ◽  
Hossein Ahmadzadeh ◽  
Elaheh K. Goharshadi
Keyword(s):  
Gel Electrophoresis ◽  
Heat Dissipation ◽  
Separation Efficiency ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sio2 Nanoparticles ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Sds Page ◽  
Separation Of Proteins ◽  
Gel Network

Tethered nanoparticles (NPs) are able to improve the separation efficiency of proteins in SDS-polyacrylamide gel electrophoresis (SDS-PAGE) due to their capability of enhancing heat dissipation during electrophoresis and restriction of electrophoretic movement of NPs.

[15] Very-high-resolution two-dimensional electrophoretic separation of proteins on giant gels

1983 ◽  
pp. 190-214 ◽  
Author(s):  
Donald A. Young ◽  
Bruce P. Voris ◽  
Edward V. Maytin ◽  
Robert A. Colbert
Keyword(s):  
High Resolution ◽  
Two Dimensional ◽  
Electrophoretic Separation ◽  
Separation Of Proteins ◽  
Very High

Determination of Proteins in Biological Fluids by Electroimmunodiffusion and Two-Directional Immunoelectrophoresis

1971 ◽  
Vol 17 (8) ◽  
pp. 745-750 ◽  
Author(s):  
Vidmantas A Raisys ◽  
Dean A Arvan
Keyword(s):  
High Resolution ◽  
Lower Limit ◽  
Biological Fluids ◽  
Electrophoretic Separation ◽  
Simple Apparatus ◽  
Α2 Macroglobulin ◽  
Sensitive Tool ◽  
Separation Of Proteins

Abstract We have used electroimmunodiffusion and two-directional immunoelectrophoresis to measure proteins in biological fluids. Electroimmunodiffusion is based on the electrophoresis of antigens in antibody-containing agarose under standardized conditions. Pre-albumin, albumin, α1antitrypsin, α2-macroglobulin, IgG, IgA, IgM, IgD, and other proteins have been determined in our laboratory with a precision of ±5%. The lower limit for quantitation is 5 µg/ml. For immunoglobulin quantitation, treatment of the samples with potassium cyanate (carbamylation) before electrophoresis improves sensitivity and accuracy. Two-directional immunoelectrophoresis is based on electrophoretic separation of proteins in agarose or other high-resolution media followed by electrophoresis at right angles to the first direction, in a gel in which an appropriate antiserum has been incorporated. Qualitative and semiquantitative changes in proteins in abnormal specimens can be assessed. The two techniques combined provide a very sensitive tool for the evaluation of protein changes in biologic fluids. A simple apparatus has been designed in which a number of specimens can be analyzed simultaneously by either method.

scholarly journals Identification of outbreak-associated and other strains ofClostridium difficileby numerical analysis of SDS-PAGE protein patterns

1994 ◽  
Vol 113 (1) ◽  
pp. 1-12 ◽  
Author(s):  
M. Costas ◽  
B. Holmes ◽  
M. Ganner ◽  
S. L. W. On ◽  
P. N. Hoffman ◽  
...  
Keyword(s):  
Numerical Analysis ◽  
High Resolution ◽  
Clostridium Difficile ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Patterns ◽  
One Dimensional ◽  
Sds Page

SUMMARYSeventy-three cultures ofClostridium difficileisolated both during, and in the period immediately following, an outbreak of infection in a group of three hospitals, were characterized by one-dimensional sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) of whole-cell proteins. Each protein pattern was characterized by the presence of one or two dense bands which were highly reproducible. The protein patterns were used as the basis for a numerical analysis which divided the strains into five phenons (electrophoretic or EP types). The majority, 60 of the 73 cultures, belonged to a single phenon which included strains from both patients and the environment. We conclude that high-resolution SDS–PAGE of proteins provides an effective method for typingC. difficileand therefore for tracing the possible spread of epidemic strains in hospitals and other institutions, thereby allowing a better understanding of the epidemiology of the organism.

Rapid sodium dodecyl sulfat/polyacrylamide gel electrophoresis of urinary proteins.

1980 ◽  
Vol 26 (11) ◽  
pp. 1588-1590 ◽  
Author(s):  
C Cachera ◽  
C Mizon ◽  
J C Fruchart ◽  
J Mizon ◽  
A Tacquet
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Precipitation Method ◽  
Electrophoretic Separation ◽  
Urinary Proteins ◽  
Special Apparatus ◽  
Separation Of Proteins

Abstract We describe a procedure for the convenient separation of proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of urine from cases of renal disease. A precipitation method that requires no special apparatus was used to concentrate the urinary proteins; for electrophoretic separation we used a commercially supplied polyacrylamide/cellulose gel slab. This method seems to be valuable for investigation of proteinuria; we recommend it for routine use.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia

1985 ◽  
Vol 54 (03) ◽  
pp. 626-629 ◽  
Author(s):  
M Meyer ◽  
F H Herrmann
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Type Ii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Structural Variant ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Proteins

SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surface iodination. In unreduced-reduced two-dimensional gel electrophoresis two components were observed in the region of GP Ilia. The assumption of a structural variant of GP Ilia in the two related patients is discussed.

Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

2018 ◽  
Vol 26 (2) ◽  
pp. 058
Author(s):  
Anna P. Roswiem ◽  
Triayu Septiani
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page

<em>Bahan<strong> </strong>baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE).<strong> </strong>Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi  dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.</em>

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