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 Purification and characterization of a labile rat glutathione transferase of the Mu class

1989 ◽  
Vol 260 (3) ◽  
pp. 789-793 ◽  
Author(s):  
A Kispert ◽  
D J Meyer ◽  
E Lalor ◽  
B Coles ◽  
B Ketterer
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Glutathione Transferase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Residues ◽  
Purification And Characterization ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Cnbr Cleavage

A labile GSH transferase homodimer termed 11-11 was purified from rat testis by GSH-agarose affinity chromatography followed by anion-exchange f.p.l.c. The enzyme is unstable in the absence of thiol(s) and has relatively low affinity for both 1-chloro-2,4-dinitrobenzene (Km 4.4 mM) and GSH (Km(app.) 4.4mM). Its mobility on SDS/polyacrylamide-gel electrophoresis is slightly less than that of subunits 3 and 4 and its pI is 5.2. Subunit 11 has a blocked N-terminal amino acid residue, but after CNBr cleavage fragments accounting for 113 amino acid residues were sequenced and showed 65% homology with corresponding sequences in subunit 4, indicating that it is a member of the Mu family. GSH transferase 11 is a major isoenzyme in testis, epididymis, prostate and brain and present at lower concentrations in other tissues.

scholarly journals Purification of a phosphoprotein from chromatin of rat liver

1979 ◽  
Vol 183 (1) ◽  
pp. 147-156 ◽  
Author(s):  
P K Chan ◽  
C C Liew
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Basic Amino Acid ◽  
Phosphate Content ◽  
Acid Ratio ◽  
Chromatin Proteins

A simple and effective method to purify a phosphoprotein (B2) (Mr 68,000, pI 6.2-8) from phenol-soluble non-histone chromatin proteins of rat liver is described. The purification involved only two steps, CM-cellulose chromatography and preparative SDS/polyacrylamide (10%)-gel electrophoresis. The purified phosphoprotein B2 was shown to be homogeneous by SDS/polyacrylamide-gel electrophoresis. The yield was 2% of total non-histone chromatin proteins. The acidic to basic amino acid ratio of phosphoprotein B2 was less than 1, with high contents of glutamic acid, aspartic acid, arginine, lysine, glycine and alanine. The phosphate content of this protein is 0.3%.

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.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

Characterization of antithrombin III from human plasma by two-dimensional gel electrophoresis and capillary electrophoretic methods

2003 ◽  
Vol 24 (24) ◽  
pp. 4282-4290 ◽  
Author(s):  
Leopold Kremser ◽  
Andrea Brückner ◽  
Andrea Heger ◽  
Tom Grunert ◽  
Andrea Buchacher ◽  
...  
Keyword(s):  
Human Plasma ◽  
Gel Electrophoresis ◽  
Antithrombin Iii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Capillary Electrophoretic
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