Analysis of Proteinuria Using a Commercial System for Automated Electrophoresis and Isoelectric Focusing

1988 ◽  
Vol 25 (3) ◽  
pp. 319-324 ◽  
Author(s):  
P J Jackson ◽  
C J Sampson ◽  
E H Cooper ◽  
D Heney ◽  
J T Brocklebank
Keyword(s):  
Isoelectric Focusing ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tubular Dysfunction ◽  
Urinary Proteins ◽  
Sds Page ◽  
Glomerular Damage ◽  
Bence Jones Proteins

We describe an investigation of proteinuria using Pharmacia PhastSystem™ electrophoresis apparatus. The analysis of urinary proteins by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) of unconcentrated urine followed by silver staining took about 2 h and could clearly demonstrate tubular dysfunction or glomerular damage in urines with a negative or only trace-positive dip-stick test for protein. In addition, we show the identification of urinary proteins by immunoblotting from SDS-PAGE gels and the characterisation of Bence-Jones proteins by isoelectric focusing (IEF) and immunoblotting.

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 Purification and properties of succinyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney

1978 ◽  
Vol 173 (3) ◽  
pp. 759-765 ◽  
Author(s):  
J A Sharp ◽  
M R Edwards
Keyword(s):  
Isoelectric Focusing ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Coenzyme A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Polyacrylamide Gel ◽  
Transferase Activity ◽  
Coa Transferase

CoA-transferase (succinyl-CoA-3-oxo acid CoA-transferase, EC 2.8.3.5) isolated from sheep kidney was purified to homogeneity. The purified enzyme has a specific activity of approx. 200 units/mg. A mol.wt. of 110000 was obtained by gel filtration on Sephadex G-200, and a lower mol.wt. of 102000 was determined by analytical ultracentrifugation. A sedimentation coefficient of 5.6S was also determined. A subunit mol.wt. of 56000 was obtained by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Isoelectric focusing of sheep kidney extracts indicated the presence of a single band of CoA-transferase activity with pI9.0. However, isoelectric focusing of purified CoA-transferase showed the presence of two peaks of CoA-transferase activity with pI values of 8.7 and 8.4, suggesting the presence of proteolytic activity during purification. Evidence for sheep kidney CoA-transferase being a dimer of two identical subunits has been obtained from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the amino acid composition, peptide ‘mapping’ and N-terminal analysis.

scholarly journals Mapping of the genes controlling high-molecular-weight glutelin subunits of rye on the long arm of chromosome 1R

1984 ◽  
Vol 44 (2) ◽  
pp. 117-123 ◽  
Author(s):  
N. K. Singh ◽  
K. W. Shepherd
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Translocation Line ◽  
Sds Page ◽  
Chromosome 1R

SUMMARYThe gene(s) controlling the high-molecular-weight glutelin subunits in rye (designated as Glu-Rl) was mapped with respect to the centromere using a 1RL-1DS wheat-rye translocation line and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Analysis of 479 seeds from test-crosses between a 1R/1RL-1DS heterozygote and the cultivar India 115, revealed 14·6% aneuploid and 3·95% recombinant progeny. Excluding the aneuploids, this locus was calculated to be 4·65 ± 1·04 cM from the centromere on the long arm of chromosome 1R, which is comparable to the position of the homoeologous loci in wheat and barley.

Acid and alkaline phosphatases of Capnocytophaga species. II. Isolation, purification, and characterization of the enzymes from Capnocytophaga ochracea

1983 ◽  
Vol 29 (10) ◽  
pp. 1361-1368 ◽  
Author(s):  
Thomas P. Poirier ◽  
Stanley C. Holt
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Alkaline Phosphatases ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Sds Page ◽  
Kinetics Of

Capnocytophaga ochracea acid (AcP; EC 3.1.3.2) and alkaline (AlP; EC 3.1.3.1) phosphatase was isolated by Ribi cell disruption and purified by sodium dodecyl sulphate – polyacrylamide gel electrophoresis (SDS–PAGE.) Both phosphatases eluted from Sephadex G-150 consistent with molecular weights (migration) of 140 000 and 110 000. SDS–PAGE demonstrated a 72 000 and 55 000 subunit molecular migration for AcP and AlP, respectively. The kinetics of activity of purified AcP and AIP on p-nitrophenol phosphate and phosphoseryl residues of the phosphoproteins are presented.

PROFIL PROTEIN VAKSIN Aeromonas hydrophila DAN Streptococcus agalactiae HASIL INAKTIVASI DENGAN FORMALIN: DIUJI MENGGUNAKAN Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 9 (3) ◽  
pp. 449
Author(s):  
Desy Sugiani ◽  
Angela Mariana Lusiastuti ◽  
Sukenda Sukenda ◽  
Enang Harris
Keyword(s):  
Streptococcus Agalactiae ◽  
Sodium Dodecyl Sulphate ◽  
Total Protein ◽  
Aeromonas Hydrophila ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page ◽  
Neutral Buffer Formalin

Vaksin bakterin dalam bentuk protein merupakan salah satu tipe vaksin yang telah banyak dikembangkan. Protein digunakan sebagai vaksin biasanya dibuat dengan teknik inaktivasi formalin-killed. Vaksin ini biasanya lebih mudah dibuat, lebih murah, lebih stabil, dan mampu disimpan dalam waktu lama. Akan tetapi masih sedikit informasi mengenai efek perlakuan tersebut terhadap profil protein. Pada penelitian ini, untuk mengevaluasi profil protein, dilakukan inaktivasi sediaan vaksin dari isolat bakteri Aeromonas hydrophila AHL0905-2 dan Streptococcus agalactiae N14G dengan menambahkan 0,5% formalin dan 3% neutral buffer formalin (NBF) ke dalam biakan plasebo bakterin dan diinkubasi selama 24 jam. Kualitas produk vaksin ditentukan berdasarkan uji karakterisasi protein menggunakan metode Bradford dan SDS-PAGE. Hasil uji menunjukkan bahwa sediaan vaksin A. hydrophila dan S. agalactiae yang diinaktivasi dengan 3% NBF memiliki profil protein lebih variatif dibandingkan dengan sediaan vaksin yang diinaktivasi dengan 0,5% formalin. Akan tetapi, inaktivasi vaksin A. hydrophila dan S. agalactiae dengan 3% NBF menghasilkan berat total protein yang lebih rendah jika dibandingkan dengan dengan sediaan vaksin yang diinaktivasi dengan 0,5% formalin.

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