Identification of non-cross-reacting antigens of Onchocerca volvulus with lymphatic filariasis serum pools

Parasitology ◽  
1986 ◽  
Vol 93 (2) ◽  
pp. 389-399 ◽  
Author(s):  
E. Lobos ◽  
N. Weiss
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Lymphatic Filariasis ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
The Other ◽  
Onchocerca Volvulus ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Species Specific

SUMMARYOnchocerca volvulus proteins labelled with 125I were immunoprecipitated with onchocerciasis and lymphatic filariasis human serum pools in order to differentiate between cross-reacting and non-cross-reacting antigens. Analysis of the immunoprecipitates by two-dimensional gel electrophoresis revealed that all high molecular weight (Mr) O. volvulus antigens cross-reacted with the lymphatic filariasis serum pools. We observed, however, that at least 8 0. volvulus antigens were specifically immunoprecipitated only by the onchocerciasis serum pools, with Mr ranging from 20000 up to 43000 Daltons. These results suggest that the lower MrO. volvulus antigens are more species specific than the other antigens. The significance of these findings for the immunodiagnosis of onchocerciasis is discussed.

scholarly journals Variations in the Methionine-rich Protein Composition of the Genus Arachis1

1984 ◽  
Vol 11 (1) ◽  
pp. 1-3 ◽  
Author(s):  
Sheikh M. Basha ◽  
Sunil K. Pancholy
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Protein Composition ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Weight Group ◽  
Two Dimensional Gel Electrophoresis ◽  
One Dimensional ◽  
Molecular Weights ◽  
Isoelectric Points

Abstract Methionine-rich proteins (MRP) from seeds of different species of the Genus Arachis were isolated and analyzed by gel electrophoresis to detect possible compositional differences. One-dimensional gel electrophoretic analysis showed presence of quantitative and qualitative variations among the MRP-fractions. Following two-dimensional gel electrophoresis, the MRP-fractions were found to contain three groups of polypeptides with apparent molecular weights of approximately 21,000; 19,000 and 16,000, and isoelectric points between 5.1 and 5.8. Within each molecular weight group the number of polypeptides varied between 1 and 3.

Protein Synthesis During Oxygen Deprivation in Cotton

1996 ◽  
Vol 23 (3) ◽  
pp. 341 ◽  
Author(s):  
AA Millar ◽  
ES Dennis
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Major Part ◽  
Oxygen Deprivation ◽  
Two Dimensional ◽  
Root Tips ◽  
Two Dimensional Gel Electrophoresis ◽  
Molecular Masses ◽  
Adh Activity

The alteration of protein synthesis induced by oxygen deprivation has been examined in the root tips of cotton (Gossypium hirsutum cv. Siokra), a plant that is intolerant to anoxia. Using [35S]methionine labelling and two-dimensional gel electrophoresis it was demonstrated that 14 major polypeptides are being selectively synthesised during oxygen deprivation. These polypeptides have been designated the cotton anaerobic polypeptides (ANPs), and have estimated molecular masses that correspond to molecular masses of ANPs from other plant species. However, compared to maize, several of the major molecular weight classes are absent, suggesting that the response to oxygen deprivation in cotton is simpler than that of maize. Alcohol dehydrogenase (ADH) activity is induced by oxygen deprivation. Using western analysis we have determined that this increase in activity is correlated with the accumulation of the ADH polypeptide and that three of the major cotton ANPs are ADH, including the most intensely labelled ANP, demonstrating that the synthesis of ADH constitutes a major part of the response in cotton.

Fibrin-I Degradation Products with a Molecular Weight Higher than That of Fibrinogen

1973 ◽  
Vol 29 (01) ◽  
pp. 122-129 ◽  
Author(s):  
René von Hugo ◽  
Henner Graeff
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Degradation Products ◽  
Gel Filtration ◽  
Agarose Gel ◽  
Two Dimensional ◽  
Plasma Clot ◽  
Two Dimensional Gel Electrophoresis ◽  
Parent Molecule

SummaryThe observation of intravascular lysis of fibrin deposits and of fibrinogen derivatives with a molecular weight higher than the parent molecule in human cases of disseminated intravascular coagulation (DIC) initiated the following in vitro study. Following streptokinase induced plasma clot solubilization fibrinogen derivatives were investigated after ß-alanine precipitation of the plasma samples by polyacrylamide (PAA) gel electrophoresis, intra gel immunoprecipitation, two dimensional gel electrophoresis and by agarose gel filtration. Three fibrin-i degradation products were observed and characterized according to their relative electrophoretic mobility in 5% PAA gel: 0.23, 0.35, 0.46 (fibrinogen: 0.43) x 10-5 cm2/V x sec. They could also be demonstrated after electrophoresis in the presence of 5 M urea. Agarose gel filtration yielded one peak at 180 ml of effluent volume. The 0.23 derivative was eluted in the peak fractions, whilst the 0.35 and 0.46 derivatives were eluted together at approximately 201 ml of the effluent volume (fibrinogen: 225 ml). This indicates, that the three fibrin-i degradation products described are molecular entities with molecular weights higher than fibrinogen and, that the 0.46 derivative has an increased charge/molecular size ratio in comparison with fibrinogen. Corresponding data were obtained by two dimensional gel electrophoresis in gels of different pore size.

Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

1995 ◽  
Vol 16 (1) ◽  
pp. 851-853 ◽  
Author(s):  
Barbara Marzocchi ◽  
Barbara Magi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

scholarly journals Two-dimensional gel electrophoresis detects prostate-specific antigen–α1-antichymotrypsin complex in serum but not in prostatic fluid

1997 ◽  
Vol 43 (2) ◽  
pp. 352-359 ◽  
Author(s):  
Yi Qian ◽  
Julia A Sensibar ◽  
David J Zelner ◽  
Anthony J Schaeffer ◽  
Judith A Finlay ◽  
...  
Keyword(s):  
Western Blot ◽  
Human Serum ◽  
Prostate Specific Antigen ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Specific Antigen ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Prostatic Fluid ◽  
Three Body

Abstract We investigated the interaction between prostate-specific antigen (PSA) and 1-antichymotrypsin (ACT) in prostatic secretions, identifying PSA and ACT in human serum, prostatic fluid, and seminal plasma by two-dimensional gel electrophoresis (2-D PAGE). Both PSA and ACT were detected in all three body fluids, but PSA-ACT complex was detected only in serum. Moreover, the 2-D PAGE Western blot staining profile for ACT from serum differed from that for prostatic fluid or seminal plasma. Incubation of prostatic fluid with purified ACT led to formation of PSA-ACT complex. Incubation of prostatic fluid with purified PSA, however, failed to form the complex, suggesting that the ACT in prostatic fluid was inactive or inhibited. Given that physiological concentrations of zinc inhibited the formation of PSA-ACT complex, we consider zinc a possible physiological inhibitor of the formation of the PSA-ACT complex. These results indicate that the failure to detect the PSA-ACT complex in prostatic fluid could be related to the inactivation of ACT, the presence of inhibitors (e.g., zinc), or simply the PSA:ACT ratio in the fluid.

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