scholarly journals Specific proteins synthesized during the viral lytic cycle in vaccinia virus-infected HeLa cells: analysis by high-resolution, two-dimensional gel electrophoresis.

1986 ◽  
Vol 58 (2) ◽  
pp. 569-577 ◽  
Author(s):  
L Carrasco ◽  
R Bravo
Keyword(s):  
High Resolution ◽  
Vaccinia Virus ◽  
Hela Cells ◽  
Gel Electrophoresis ◽  
Lytic Cycle ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Specific Proteins

Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia

1985 ◽  
Vol 54 (03) ◽  
pp. 626-629 ◽  
Author(s):  
M Meyer ◽  
F H Herrmann
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Type Ii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Structural Variant ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Proteins

SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surface iodination. In unreduced-reduced two-dimensional gel electrophoresis two components were observed in the region of GP Ilia. The assumption of a structural variant of GP Ilia in the two related patients is discussed.

A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells

1993 ◽  
Vol 104 (3) ◽  
pp. 629-638 ◽  
Author(s):  
H. Hattori ◽  
T. Kaneda ◽  
B. Lokeshwar ◽  
A. Laszlo ◽  
K. Ohtsuka
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Gel Electrophoresis ◽  
Recovery Period ◽  
Chinese Hamster ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Terminal Amino ◽  
Kinetics Of

We have previously reported that a novel 40 kDa protein is induced by heat shock and several environmental stresses in mammalian and avian cells and that the N-terminal amino acid sequence of this 40 kDa protein has homology with the bacterial DnaJ heat-shock protein. We have purified this protein (40 kDa heat-shock protein, hsp40) from HeLa cells by modified two-dimensional gel electrophoresis and generated a polyclonal antibody against hsp40. This antibody was highly specific for human hsp40 and cross-reacted weakly with rat and Chinese hamster hsp40. Indirect immunofluorescence revealed that the hsp40 in HeLa cells accumulates in the nucleus, especially in the nucleolus, during heat shock and returns to the cytoplasm during the recovery period. The kinetics of the accumulation in the nucleoli and subsequent return to the cytoplasm of hsp40 was similar to that of hsp70. In addition, hsp40 was co-localized with hsc70(p73) in heat-shocked HeLa cells as demonstrated by double immunofluorescence staining. These results suggest that hsp40 (a DnaJ homologue) and hsp70 (a DnaK homologue) may act in concert to repair (refold) denatured proteins and protein aggregates in the nuclei and nucleoli of heat-shocked HeLa cells.

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.

Technology: Methodology for High-Resolution Two-Dimensional Gel Electrophoresis

1987 ◽  
Vol 5 (2) ◽  
pp. 127-149 ◽  
Author(s):  
A Thomas Endler ◽  
Donald S. Young ◽  
Russell P. Tracy
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis
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