scholarly journals Use of DNA Ladders for Reproducible Protein Fractionation by Sodium Dodecyl Sulfate−Polyacrylamide Gel Electrophoresis (SDS−PAGE) for Quantitative Proteomics

2008 ◽  
Vol 7 (2) ◽  
pp. 678-686 ◽  
Author(s):  
Guoan Zhang ◽  
David Fenyö ◽  
Thomas A. Neubert
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Quantitative Proteomics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Protein Fractionation ◽  
Sds Page ◽  
Dodecyl Sulfate

scholarly journals Differentiation of Bartonella Species by a Microimmunofluorescence Assay, Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis, and Western Immunoblotting

2000 ◽  
Vol 7 (4) ◽  
pp. 617-624 ◽  
Author(s):  
Zhongxing Liang ◽  
Didier Raoult
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Bartonella Henselae ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Pairwise Comparison ◽  
Polyacrylamide Gel ◽  
Sds Page ◽  
Dodecyl Sulfate ◽  
Parsimony Trees

ABSTRACT Bartonella species can be differentiated by microimmunofluorescence assay, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and immunoblotting with murine polyclonal antisera to Bartonella henselae, B. quintana, B. elizabethae, and B. bacilliformis. A pairwise comparison on the basis of SDS-PAGE protein profiles demonstrated similarity values for proteins of different Bartonella species ranging from 28.6 to 86.4%. Antigenic relationships revealed by immunoblotting with murine antisera were equivalent to those of proteins observed by SDS-PAGE. A dendrogram obtained on the basis of protein bands of SDS-polyacrylamide gels showed that Bartonella species could be divided into three groups. B. bacilliformis was distinct from all otherBartonella species; B. grahamii, B. taylorii, B. doshiae, and B. vinsoniiformed a cluster, as did B. henselae, B. quintana, B. elizabethae, and B. clarridgeiae. These relationships were consistent with those revealed by parsimony trees derived from 16S rRNA and gltAgene sequencing. SDS-PAGE analysis showed that 120-, 104-, 85-, 71-, 54-, 47-, 40-, 33-, 30-, and 19-kDa proteins were present in all species, with the 54-kDa protein being the most dominant. Proteins with a molecular mass of less than 54 kDa allow the differentiation of species and are a possible target for future species-specific antibodies and antigens.

scholarly journals Pre-Screening Profil Protein Daging Sebagai Pengaruh Variasi Metode Penyembelihan Hewan

WARTA AKAB ◽  
2021 ◽  
Vol 44 (2) ◽  
Author(s):  
Alvina Nur Aini
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page ◽  
Dodecyl Sulfate

Perbedaan proses penyembelihan dapat mempengaruhi respon fisiologis hewan yang dapat diidentifikasi melalui pola ekspresi protein. Dalam penelitian ini dilakukan analisis awal protein daging untuk menganalisis pengaruh perbedaan metode penyembelihan, yaitu metode halal dan nonhalal. Penelitian menggunakan enam ekor tikus Wistar sebagai hewan uji. Kelompok uji pertama diberi perlakuan penyembelihan dengan metode halal, yaitu dengan pemotongan pembuluh darah pada leher hewan. Kelompok kedua diberi perlakuan penyembelihan secara nonhalal, yaitu dilakukan metode dislokasi servikal. Analisis profil protein daging dilakukan dengan menggunakan Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Hasil SDS-PAGE menunjukkan beberapa pita protein tereskpresi pada berat molekul 116; 55; 48; 45; 41; 26; dan 17 kDa (kiloDalton), sedangkan hasil kuantifikasi pita protein menunjukkan sampel protein daging hasil penyembelihan nonhalal memiliki kuantitas lebih tinggi daripada sampel protein daging hasil penyembelihan halal. Kuantitas protein yang lebih tinggi pada penyembelihan nonhalal diduga karena lepasnya protein tertentu ke dalam sistem metabolisme hewan sebagai akibat dari respon stres yang diberikan.Kata kunci: elektroforesis; halal; nonhalal; protein; SDS-PAGE

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