Analysis for Cerebrospinal Fluid Proteins by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

1992 ◽  
Vol 38 (10) ◽  
pp. 2008-2012 ◽  
Author(s):  
F Mashige ◽  
T Shimizu ◽  
S Iijima ◽  
A Ohkubo

Abstract Cerebrospinal fluid (CSF) proteins with molecular masses of < 150,000 Da were identified by immunoblotting after two kinds of nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). With PAGE 1 (17-27% gradient gel), CSF proteins were clearly separated into seven to nine bands with molecular masses of 3000-67,000 Da; seven bands were identified as beta 2-microglobulin, lysozyme, prealbumin, free kappa and lambda chain, apolipoprotein A-I, glycoproteins, and albumin by immunoblotting. With PAGE 2 (10-20% gradient gel), proteins were clearly separated into 11-16 bands with molecular masses of 15,000-150,000 Da; 11 were identified as prealbumin, free kappa and lambda chain, apolipoprotein A-I, glycoproteins, albumin, alpha 1-antitrypsin, transferrin (separated into two bands), immunoglobulin fragments, haptoglobin, and IgG. We analyzed CSF samples collected from 81 patients with cerebrospinal signs by these SDS-PAGE methods and observed prominent bands in some cases.

2000 ◽  
Vol 7 (4) ◽  
pp. 617-624 ◽  
Author(s):  
Zhongxing Liang ◽  
Didier Raoult

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.


Plant Disease ◽  
1998 ◽  
Vol 82 (2) ◽  
pp. 210-212 ◽  
Author(s):  
Harry H. Kope ◽  
Abul K. M. Ekramoddoullah ◽  
Jack R. Sutherland

Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of crude extracts of disease-free and Didymascella thujina-infected foliage of western red-cedar revealed differences in several protein bands and suggests that distinct proteins of D. thujina origin can be identified by SDS-PAGE.


WARTA AKAB ◽  
2021 ◽  
Vol 44 (2) ◽  
Author(s):  
Alvina Nur Aini

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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