scholarly journals Clustering of Clinical Strains ofHelicobacter pylori Analyzed by Two-Dimensional Gel Electrophoresis

2000 ◽  
Vol 7 (2) ◽  
pp. 301-306 ◽  
Author(s):  
Helena Enroth ◽  
Thomas Åkerlund ◽  
Anna Sillén ◽  
Lars Engstrand
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Two Dimensional ◽  
Strain Variation ◽  
Disease Group ◽  
Two Dimensional Gel Electrophoresis ◽  
Specific Proteins ◽  
Patient Groups ◽  
H Pylori ◽  
Disease Specific

ABSTRACT Strain variations of Helicobacter pylori have been tested by numerous methods and compared among different patient groups. The aim of this study was to investigate whether H. pyloriexpresses disease-specific proteins that can be detected by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). H. pylori strains isolated from duodenal ulcer, gastric cancer, and gastritis patients were analyzed. Extensive variation in spot patterns was observed between the strains, but a dendrogram analysis revealed that some strains within each disease group clustered together. Eight proteins were sequenced and found in the H. pylori genome sequence. 2-D PAGE is a useful method for studies of protein expression and for highlighting the extensive strain variation that H. pylori exhibits.

Analysis of the cytosolic proteins of chick embryo gonads by two-dimensional gel electrophoresis

Development ◽  
1986 ◽  
Vol 94 (1) ◽  
pp. 221-230
Author(s):  
J. Samsel ◽  
B. Lorber ◽  
A. Petit ◽  
J. -P. Weniger
Keyword(s):  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Protein ◽  
Chick Embryos ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Specific Proteins ◽  
Different Tissues

Gonads and mesonephros dissected from normal chick embryos, as well as a blood sample, were labelled in vitro with [35S]methionine and [14C]leucine. The patterns of cytosolic protein synthesis of the different tissues were analysed using two-dimensional (2-D) polyacrylamide gel electrophoresis. Three developmental stages, i.e. 8, 12 and 17 days of incubation, were investigated. Five sex-specific proteins were detected in the male and two in the female. In the testis, only one protein is already present at the 8-day stage. In the ovary, one protein exists since the 8-day stage, but it is also synthesized in the mesonephros. The second ovary-specific protein appeared only at the 12-day stage.

A New Method for Proteome Screening with Two-Dimensional Urea-Sds Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Areeba Ahmad ◽  
Riaz Ahmad
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cost Effective ◽  
Polyacrylamide Gel ◽  
Present System ◽  
Liver Protein ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

AbstractTwo-dimensional gel electrophoresis (2DE) separating proteins on the basis of their pI and molecular mass remain the best available technique for protein separation and characterization to date. But due to several limitations, including streak formation in IEF gels, partial solubility of proteins, expensive running conditions and relatively longer time taken, a simple urea-SDS-2D polyacrylamide gel electrophoresis (US2DE) is described here. The system is reasonably sensitive, cost effective with good reproducibility. The method described in this paper employs a chaotropic agent, urea, in the first dimension and sodium dodecyl sulphate (SDS), like conventional system, in the second dimension with an addition of polyacrylamide to screen the liver proteome of healthy and chemically induced fibrotic rats. The system separates the protein on the basis of chargeto- mass ratio and clearly demonstrates differential expression in the liver protein repertoire of healthy and fibrotic rats. Moreover, the present system, like other 2D electrophoretic procedures revealed at least 22 novel spots in the investigated tissues. The technique may be utilized for comprehensive proteome screening of any biological sample and would provide an overview to narrow down the candidate proteins or biomarkers.

scholarly journals Identification of Potential Diagnostic and Vaccine Candidates ofHelicobacter pylori by Two-Dimensional Gel Electrophoresis, Sequence Analysis, and Serum Profiling

1998 ◽  
Vol 5 (4) ◽  
pp. 537-542 ◽  
Author(s):  
C. Patrick McAtee ◽  
Moon Young Lim ◽  
Kevin Fung ◽  
Mark Velligan ◽  
Kirk Fry ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Gel Electrophoresis ◽  
Vaccine Development ◽  
Two Dimensional ◽  
Terminal Sequence ◽  
Two Dimensional Gel Electrophoresis ◽  
Western Blots ◽  
Vaccine Candidates ◽  
Serum Profiling ◽  
H Pylori

ABSTRACT There is great interest in characterizing the proteins of the gastric pathogen Helicobacter pylori, especially those to which humans respond immunologically, because of the potential importance of such proteins in diagnosis and vaccine development. Two-dimensional gel electrophoresis was used to separate and identify potential antigens of H. pylori ATCC 43504. Over 30 proteins were reactive in Western blots with pooled sera from 14 infected patients. These proteins were analyzed by N-terminal sequence analysis. Fourteen proteins were determined to be distinct from any proteins previously described from H. pylori; the others were previously isolated and characterized proteins. Analysis of eight distinct H. pylori strains showed that most of these antigens were produced by all of the strains. We propose that collection of new antigens such as those recognized here will be useful in serologic tests for detecting and monitoring H. pylori infection and may also serve as potential targets for antimicrobial agent or vaccine development.

scholarly journals Proteomic Characterisation of Lupin (Lupinus angustifolius) Milk as Influenced by Extraction Techniques, Seed Coat and Cultivars

Molecules ◽  
2020 ◽  
Vol 25 (8) ◽  
pp. 1782
Author(s):  
Nadia Al-Saedi ◽  
Manjree Agarwal ◽  
Wujun Ma ◽  
Shahidul Islam ◽  
Yonglin Ren
Keyword(s):  
Gel Electrophoresis ◽  
Milk Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Two Dimensional ◽  
Extraction Techniques ◽  
Centrifuge Method ◽  
Lupin Seeds ◽  
Specific Proteins ◽  
Protein Extractability ◽  
Better Than

Lupin seeds are rich in proteins and other essential ingredients that can help to improve human health. The protein contents in both whole and split seeds of two lupin cultivars (Mandleup and PBA Jurien) were used to produce the lupin milk using the cheesecloth and centrifuge method. Proteins were extracted from the lupin milk using thiourea/urea solubilization. The proteins were separated by a two-dimensional polyacrylamide gel electrophoresis and then identified with mass spectrometry. A total of 230 protein spots were identified, 60 of which showed differential abundances. The cheesecloth separation showed protein extractability much better than that of the centrifuge method for both the cultivars. The results from this study could offer guidance for future comparative analysis and identification of lupin milk protein and provide effective separation technique to determine specific proteins in the cheese-making process.

scholarly journals Identification of Proteins Related to Nickel Homeostasis in Helicobater pylori by Immobilized Metal Affinity Chromatography and Two-Dimensional Gel Electrophoresis

2008 ◽  
Vol 2008 ◽  
pp. 1-6 ◽  
Author(s):  
Xuesong Sun ◽  
Ruiguang Ge ◽  
Jen-Fu Chiu ◽  
Hongzhe Sun ◽  
Qing-Yu He
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Interacting Proteins ◽  
Peptic Ulcers ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Iron Storage ◽  
Cell Extracts ◽  
Nickel Homeostasis ◽  
H Pylori

Helicobacter pylori (H. pylori) is a widespread human pathogen causing peptic ulcers and chronic gastritis. Maintaining nickel homeostasis is crucial for the establishment of H. pylori infection in humans. We used immobilized-nickel affinity chromatography to isolate Ni-related proteins from H. pylori cell extracts. Two-dimensional gel electrophoresis and mass spectrometry were employed to separate and identify twenty two Ni-interacting proteins in H. pylori. These Ni-interacting proteins can be classified into several general functional categories, including cellular processes (HspA, HspB, TsaA, and NapA), enzymes (Urease, Fumarase, GuaB, Cad, PPase, and DmpI), membrane-associated proteins (OM jhp1427 and HpaA), iron storage protein (Pfr), and hypothetical proteins (HP0271, HP jhp0216, HP jhp0301, HP0721, HP0614, and HP jhp0118). The implication of these proteins in nickel homeostasis is discussed.

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.

Two-dimensional gel electrophoresis of cerebrospinal fluid proteins.

1980 ◽  
Vol 26 (9) ◽  
pp. 1317-1322 ◽  
Author(s):  
D Goldman ◽  
C R Merril ◽  
M H Ebert
Keyword(s):  
Cerebrospinal Fluid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Spinal Fluid ◽  
Two Dimensional ◽  
Silver Stain ◽  
Two Dimensional Gel Electrophoresis ◽  
Cerebrospinal Fluid Proteins ◽  
High Resolution Analysis

Abstract Two-dimensional electrophoresis, with isoelectric focusing in the first dimension and sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the second, has been adapted for the high-resolution analysis of cerebrospinal fluid proteins. Proteins were detected with a new, highly sensitive silver stain that made visible more than 300 polypeptides from 60 microL of spinal fluid, in highly reproducible patterns. We have mapped these patterns, noting difference between the proteins observed in spinal fluid and plasma, and have prepared a partial map of cerebrospinal fluid proteins.

Sign in / Sign up

Export Citation Format

Share Document