scholarly journals WGA-SDS-PAGE: A lectin-based, new affinity gel electrophoresis for quantitative analysis of O-GlcNAc proteins

2019 ◽  
Vol 63 (2) ◽  
pp. 41-45
Author(s):  
Yuji Kubota ◽  
Ko Fujioka ◽  
Mutsuhiro Takekawa
Keyword(s):  
Quantitative Analysis ◽  
Gel Electrophoresis ◽  
Sds Page ◽  
Affinity Gel Electrophoresis

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).

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>

scholarly journals Characterizing Wool Keratin

2009 ◽  
Vol 2009 ◽  
pp. 1-5 ◽  
Author(s):  
Jeanette M. Cardamone ◽  
Alberto Nuñez ◽  
Rafael A. Garcia ◽  
Mila Aldema-Ramos
Keyword(s):  
Hydrogen Peroxide ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Alkaline Solutions ◽  
Biodegradable Material ◽  
Alkaline Hydrogen Peroxide ◽  
Cortical Cells ◽  
Sds Page ◽  
Fibrous Matrices ◽  
Wool Keratin

Keratin from wool is a reactive, biocompatible, and biodegradable material. As the biological structural component of skin (soft keratins) and of nails, claws, hair, horn, feathers, and scales (hard keratins) pure keratin comprises up to 90% by weight of wool. Wool was treated in alkaline solutions to extract from 68% to 82% keratin within 2 to 5 hours of exposure at . The keratin products were water-soluble and were confirmed to contain intermediate filament and microfibrillar component-proteins of fractured, residual cuticle, and cortical cells. Oxidation of wool by peroxycarboximidic acid in alkaline hydrogen peroxide produced keratin products with distinct microcrystalline structures: descaled fibers, fibrous matrices, and lyophilized powders. Morphology and confirmation of peptide functionality were documented by SEM, Amino Acid Analysis, SDS-PAGE gel electrophoresis, MALDI-TOF/TOF, and FTIR analyses. The reactivity of keratin from wool models the reactivity of keratin from low-value sources such as cattle hair.

scholarly journals Nitrotyrosine Density of Rabbit Urinary Bladder Muscle and Mucosa Measured via Western Blotting and 96-Well Plate Analysis

ISRN Urology ◽  
2012 ◽  
Vol 2012 ◽  
pp. 1-5
Author(s):  
Brittany Fitzpatrick ◽  
Catherine Schuler ◽  
Robert E. Leggett ◽  
Robert M. Levin
Keyword(s):  
Quantitative Analysis ◽  
Western Blotting ◽  
Optical Density ◽  
Tissue Concentration ◽  
Detrusor Muscle ◽  
Pvdf Membrane ◽  
Sds Page ◽  
Wash Buffer ◽  
Rabbit Bladder ◽  
Plate Analysis

Purpose. Nitrotyrosine was quantitated in rabbit bladder muscle and mucosa using two analytical systems: Western blotting analyses and a 96-well plate quantitative analysis kit. Materials and Methods. Rabbit bladder muscle and mucosa were obtained from control rabbits. For the Western analysis, the samples were loaded into a SDS page gel and then transferred to a PVDF membrane. The optical density was measured using a Kodak Scanner. Using the 96-well plate, the samples and standards were loaded, incubated with primary and secondary antibody, washed and vacuumed with 10x wash buffer three times between each incubation period. Stop buffer was added to the plate and the results were quantified via the plate reader. Results. For both muscle and mucosa tissue, the optical density readings were linear with tissue concentration; the concentration of nitrotyrosine in the mucosa was significantly higher than in the muscle. However, whereas the Western blot analysis is based on relative optical densities, the 96-well plate kit provides a truly quantitative analysis. Discussion. Mucosa tissue displayed a higher density of nitrotyrosine than did detrusor muscle tissue. This may well be due to the significantly higher metabolic activity of the mucosa compared to the muscle.

Immobilized metal-ion affinity systems for recovery and structure–function studies of proteins at molecular, supramolecular, and cellular levels

2010 ◽  
Vol 82 (1) ◽  
pp. 39-55 ◽  
Author(s):  
Rajasekar R. Prasanna ◽  
Mookambeswaran A. Vijayalakshmi
Keyword(s):  
Capillary Electrophoresis ◽  
Recombinant Proteins ◽  
Gel Electrophoresis ◽  
Metal Ion ◽  
Immobilized Metal Affinity Chromatography ◽  
Metal Affinity ◽  
Purification Technique ◽  
Affinity Gel Electrophoresis ◽  
Insight Into ◽  
Histidine Tag

Immobilized metal-ion affinity (IMA) adsorption is a collective term that is used to include all kinds of adsorptions where the metal ion serves as the characteristic and most essential part of adsorption center. Of all the IMA techniques, immobilized metal-affinity chromatography (IMAC) has been gaining popularity as the choice of purification technique for proteins. IMAC represents a separation technique that is primarily useful for proteins with natural surface exposed-histidine residues and for recombinant proteins with engineered histidine tag. This review also gives insight into other nonchromatographic applications of IMA adsorption such as immobilized metal-ion affinity gel electrophoresis (IMAGE), immobilized metal-ion affinity capillary electrophoresis (IMACE), and immobilized metal-ion affinity partitioning (IMAP).

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