Pattern of urinary proteins and peptides in patients with rheumatoid arthritis investigated with the Iso-Dalt technique.

1980 ◽  
Vol 26 (2) ◽  
pp. 201-204 ◽  
Author(s):  
P M Clark ◽  
L J Kricka ◽  
T P Whitehead
Keyword(s):  
Rheumatoid Arthritis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Rheumatoid Arthritis Group ◽  
Control Group ◽  
Urinary Proteins ◽  
Composite Pattern ◽  
The Individual ◽  
Proteins And Peptides

Abstract Characteristic differences in the pattern of urinary proteins and peptides have been found in patients with rheumatoid arthritis, compared with patterns from healthy controls. These differences have been demonstrated with a two-dimensional gel electrophoretic technique (Iso-Dalt) involving isoelectric focusing in the first dimension, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension. Using simple photographic techniques, one can obtain a composite pattern of the individual protein-stained gels for each group. Comparison of the composite patterns from the rheumatoid arthritis group and the control group revealed several proteins in the urine of the rheumatoid arthritis patients not found in the control group. Two groupings of these proteins were identified: acidic, high-Mr proteins and more basic, low-Mr proteins.

Pattern of urinary proteins and peptides in patients with rheumatoid arthritis investigated with the Iso-Dalt technique.

1980 ◽  
Vol 26 (2) ◽  
pp. 201-204
Author(s):  
P M Clark ◽  
L J Kricka ◽  
T P Whitehead
Keyword(s):  
Rheumatoid Arthritis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Rheumatoid Arthritis Group ◽  
Control Group ◽  
Urinary Proteins ◽  
Composite Pattern ◽  
The Individual ◽  
Proteins And Peptides

Abstract Characteristic differences in the pattern of urinary proteins and peptides have been found in patients with rheumatoid arthritis, compared with patterns from healthy controls. These differences have been demonstrated with a two-dimensional gel electrophoretic technique (Iso-Dalt) involving isoelectric focusing in the first dimension, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension. Using simple photographic techniques, one can obtain a composite pattern of the individual protein-stained gels for each group. Comparison of the composite patterns from the rheumatoid arthritis group and the control group revealed several proteins in the urine of the rheumatoid arthritis patients not found in the control group. Two groupings of these proteins were identified: acidic, high-Mr proteins and more basic, low-Mr proteins.

Reducing the artifacts produced by impure antisera in immunoblots of low-molecular-mass proteins in urine.

1986 ◽  
Vol 32 (5) ◽  
pp. 811-815 ◽  
Author(s):  
J M Perini ◽  
B Dehon ◽  
T Marianne ◽  
A Klein ◽  
P Roussel
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Rabbit Serum ◽  
Urinary Proteins ◽  
Dodecyl Sulfate ◽  
Triton X ◽  
Direct Use

Abstract Immunoblots of several urinary low-molecular-mass proteins can be very useful in investigations of pathological proteinuria. However, use of certain commercial antisera in such procedures leads to artifacts corresponding to nonspecific bands; e.g., immunoglobulins from nonimmunized rabbit serum may bind to human urinary proteins, and this binding is not inhibited by Triton X-100. We have developed a procedure to improve the specificity of detection of urinary low-Mr proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by immunoblotting with commercial antisera: we treat the protein blot with a mixture of mercaptoethanol and sodium dodecyl sulfate before incubation with the first antiserum. This allows direct use of commercial antisera without prior absorption of contaminating antibodies.

scholarly journals Antimalarial immunity in Saimiri monkeys. Immunization with surface components of asexual blood stages.

1984 ◽  
Vol 160 (2) ◽  
pp. 441-451 ◽  
Author(s):  
L H Perrin ◽  
B Merkli ◽  
M Loche ◽  
C Chizzolini ◽  
J Smart ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Protective Immunity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Saline Control ◽  
Control Group ◽  
Reverse Phase ◽  
Peak Parasitemia ◽  
Large Skin ◽  
Similar Peak

Plasmodium falciparum polypeptides of 200 and 140 K mol wt exposed at the surface of merozoites and/or schizonts were purified by affinity chromatography and by electroelution from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monkeys were separated into three groups of four and immunized either with one of the two polypeptides or with saline (control). After intravenous challenge with 2.5 X 10(7) P. falciparum asexual blood stages, two monkeys of the control group had to be treated and two recovered spontaneously after peak parasitemia of 9 and 11%. The four monkeys immunized with the 140 K polypeptide recovered without treatment after peak parasitemia between 1.5 and 4.5%. Monkeys immunized with the 200 K polypeptide had similar peak parasitemia except one monkey who suffered from a large skin excoriation and who recovered spontaneously after a peak parasitemia of 11%. Prechallenge sera of the immunized monkeys reacted only with the polypeptide used for immunization except for one serum of the 140 K group, which precipitated an additional polypeptide of 39 K, and a polypeptide of 31 K weakly precipitated by the four sera of monkeys immunized with the 200 K polypeptide. The relatedness between the 200 and 140 K polypeptides was investigated using tryptic digestion and reverse phase chromatography. No clear analogy was found between the two polypeptides, which suggests that immunization with either of two independent surface components of P. falciparum asexual blood stages is able to induce at least a partial protective immunity in immunized hosts.

Sign in / Sign up

Export Citation Format

Share Document