Two-Dimensional Fluorescence Difference Gel Electrophoretic Analysis ofStreptococcusmutansBiofilms

2005 ◽  
Vol 4 (6) ◽  
pp. 2161-2173 ◽  
Author(s):  
Catherine Rathsam ◽  
Ruth E. Eaton ◽  
Christine L. Simpson ◽  
Gina V. Browne ◽  
Valentina A. Valova ◽  
...  
1984 ◽  
Vol 30 (12) ◽  
pp. 1947-1949 ◽  
Author(s):  
P Motté ◽  
J M Bidart ◽  
J C Delarue ◽  
E Comoy ◽  
P Moingeon ◽  
...  

Abstract In an examination of cytosols from human breast tumors, we performed two-dimensional electrophoretic analysis. Several migration conditions were tried in a search for a homogeneous repartition of cytosolic proteins. The most workable gels were obtained with a 4.40 to 8.05 pH gradient in the first dimension and a homogeneous 125 g/L acrylamide/sodium dodecyl sulfate gel, 1 mm in thickness, in the second dimension. The practicability of this method is discussed.


1995 ◽  
Vol 269 (3) ◽  
pp. C802-C804 ◽  
Author(s):  
V. Menon ◽  
D. B. Thomason

We previously demonstrated that head-down tilt in rats decreases heart polypeptide initiation rate and proposed a mechanism whereby redistribution of the chaperone heat-shock cognate/heat-shock protein-70 (HSC/HSP-70) facilitates the phosphorylation of eukaryotic initiation factor-2 alpha (eIF-2 alpha). In this study, two-dimensional gel electrophoretic analysis of eIF-2 alpha showed no phosphorylation in control hearts. At 8 h of head-down tilt, there was a 45% increase in total eIF-2 alpha, and 79% was phosphorylated. At 18 h, eIF-2 alpha increased to 142% of control, of which 4% was phosphorylated. This is consistent with the previous study where, at 8 h, there was a 78% increase in polysomal HSC/HSP-70 and a shift in the polysome center-of-mass to lighter polysomes (indicating decreased initiation). After 18 h of suspension, polysomal HSC/HSP-70 levels were 24% relative to control, and the center-of-mass returned toward control. We conclude that the decrease in polypeptide initiation during head-down tilt is mediated by HSC/HSP-70 via phosphorylation of eIF-2 alpha.


1986 ◽  
Vol 351 ◽  
pp. 77-89 ◽  
Author(s):  
Thierry Rabilloud ◽  
Michelle Hubert ◽  
Philippe Tarroux

Genetica ◽  
1993 ◽  
Vol 91 (1-3) ◽  
pp. 183-198 ◽  
Author(s):  
James E. Fleming ◽  
Greg S. Spicer ◽  
Roger C. Garrison ◽  
Michael R. Rose

1982 ◽  
Vol 28 (4) ◽  
pp. 1067-1073 ◽  
Author(s):  
K E Willard ◽  
A K Thorsrud ◽  
E Munthe ◽  
E Jellum

Abstract Human leukocyte proteins from more than 150 patients with rheumatoid arthritis, together with age- and sex-matched controls, were analyzed by use of the ISO-DALT technique in two-dimensional polyacrylamide gel electrophoresis. Patients with ankylosing spondylitis, polymyalgia rheumatica, psoriatic arthritis, calcium tendinitis, post-infectious arthritis, and asymmetrical seronegative arthritis were also included as positive controls. Synthesis of several proteins, referred to by number as members of the "Rheuma" set, is shown to increase in the leukocyte preparations from patients with classical rheumatoid arthritis. Several of these proteins are specific to monocytes or granulocytes; others are of unknown cellular origin, but appear to be unique to rheumatoid arthritis. The Rheuma proteins appear to be indicators of disease activity, because their increased synthesis can be correlated with sedimentation rate and other clinical indices of rheumatoid disease activity.


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