Human bronchoalveolar lavage fluid: Two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins

1999 ◽  
Vol 20 (7) ◽  
pp. 1634-1645 ◽  
Author(s):  
Ruddy Wattiez ◽  
Cedric Hermans ◽  
Alfred Bernard ◽  
Oliver Lesur ◽  
Paul Falmagne
Keyword(s):  
Amino Acid ◽  
Bronchoalveolar Lavage ◽  
Gel Electrophoresis ◽  
Bronchoalveolar Lavage Fluid ◽  
Lavage Fluid ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

2012 ◽  
Vol 76 (3) ◽  
pp. 594-597 ◽  
Author(s):  
Takanari SHIGEMITSU ◽  
Yuhi SAITO ◽  
Shigeto MORITA ◽  
Shigeru SATOH ◽  
Takehiro MASUMURA
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Amino Acid Sequencing ◽  
Two Dimensional Gel Electrophoresis

Partial characterization of chromosomal proteins tightly bound to chicken erythroid DNA

1985 ◽  
Vol 63 (8) ◽  
pp. 824-829
Author(s):  
C. C. Liew ◽  
Peter C. Hentzen ◽  
Isaac Bekhor
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Basic Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues ◽  
Two Dimensional Gel Electrophoresis ◽  
Total Dna ◽  
Chromatin Proteins

Extraction of chicken reticulocyte and erythrocyte chromatins with 2 M NaCl yields a small fraction (about 5%) of the total DNA which is very tightly bound to a class of nonhistone chromatin proteins (DNA–P). This DNA fraction has previously been shown to be significantly enriched in active gene sequences. The proteins associated with reticulocyte and erythrocyte DNA–P were analyzed by two-dimensional gel electrophoresis. Reticulocyte DNA–P yield predominantly three major proteins, designated G1, G2, and G3 with relative masses of 80 000, 50 000, and 58 000, respectively. Erythrocyte DNA–P show only two proteins which appear to be similar to the reticulocyte G1 and G2 proteins, except in much reduced quantities as revealed by two-dimensional polyacrylamide gel electrophoresis. Amino acid analysis of the three reticulocyte proteins revealed that the ratio of acidic to basic amino acid residues increased in the order G1 < G2 < G3, while the respective isoelectric points also increased in that order.

scholarly journals Acute-phase protein concentration in bronchoalveolar lavage fluid from healthy horses

2020 ◽  
Vol 40 (12) ◽  
pp. 1073-1076
Author(s):  
Paula Alessandra Di Filippo ◽  
Luiza Maria F. Ribeiro ◽  
Marcos Aurélio D. Meireles ◽  
Francielli P. Gobbi ◽  
Andressa Francisca S. Nogueira
Keyword(s):  
Bronchoalveolar Lavage ◽  
Acute Phase ◽  
Immunoglobulin G ◽  
Gel Electrophoresis ◽  
Bronchoalveolar Lavage Fluid ◽  
Acute Phase Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Lavage Fluid ◽  
Polyacrylamide Gel ◽  
Sds Page

ABSTRACT: Bronchoalveolar lavage fluid (BALF) was analyzed to obtain information on leakage of acute-phase proteins from the blood into the respiratory lumen and about local synthesis. Ceruloplasmin, transferrin, albumin, α1-antitripsin, immunoglobulin G heavy, immunoglobulin G light, immunoglobulin A, haptoglobin, acidic glycoprotein, and P23 were measured in BALF from 30 horses without inflammatory disease by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). In serum, the same proteins were identified except for α1-antitrypsin. In conclusion, this study demonstrated that polyacrylamide gel electrophoresis (SDS-PAGE) can be used for the determination of acute-phase proteins in BALF samples from horses. In healthy horses, the values are very low, but they can be compared with reference values to assist in the diagnosis of animals with respiratory diseases.

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