The Experts below are selected from a list of 63 Experts worldwide ranked by ideXlab platform

Mark L. Salkie - One of the best experts on this subject based on the ideXlab platform.

  • A retrospective study of the relative utility of electrophoresis, Immunoelectrophoresis, immunofixation, and nephelometry in the investigation of serum proteins
    Clinical Biochemistry, 1996
    Co-Authors: Mark L. Salkie
    Abstract:

    Abstract Objectives: To assess the relative value of visual inspection of protein electrophoresis patterns, Immunoelectrophoresis, immunofixation, and specific protein quantitation in the investigation of serum proteins. Design and Methods: A retrospective study of protein results on 372 sera analyzed by electrophoresis and Immunoelectrophoresis. A subsection of specimens (276) also had immunoglobulin quantitation by immunonephelometry and 30 were studied by immunofixation. Results: Total gamma globulin levels were correctly assessed visually in 84.4% of cases. Discrete bands seen visually were mainly monoclonal in 74 of 80 (92.5%). Six monoclonal proteins were not detected visually. Twenty-five monoclonal proteins required immunofixation for typing, and 60 were typed by Immunoelectrophoresis. The visual assessment of the level of normal immunoglobulins in the presence of a monoclonal gammopathy was correct in 58% of cases. Conclusions: The majority of monoclonal gammopathies could be evaluated by a combination of protein electrophoresis and Immunoelectrophoresis. Except for quantitating monoclonal immunoglobins, protein electrophoresis was unreliable as a quantitative procedure and nephelometry was preferred.

A Laine - One of the best experts on this subject based on the ideXlab platform.

  • Crossed Immunoelectrophoresis.
    Methods in molecular biology (Clifton N.J.), 1992
    Co-Authors: A Laine
    Abstract:

    Ressler first described in 1960 (1) a form of Immunoelectrophoresis now called crossed Immunoelectrophoresis (CIE) or two-dimensional Immunoelectrophoresis, which was later improved by Laurell (2), Clarke and Freeman (3), and Weeke (4), among others. CIE is superior to the classical Immunoelectrophoresis, according to Grabar and Williams (5), particularly in providing better resolution and quantitative capabilities. It combines the electrophoretic separation of the sample proteins in agarose gel with electrophoresis at right angles to the initial separation in an antibody-containing agarose. Each protein separated during the first dimension forms a separate precipitation peak during the second dimension. Moreover, the area under any protein peak is directly proportional to the concentration of that protein in the analyzed sample and inversely proportional to the concentration of antibody to that protein in the antiserum used.

Andrew D Goetz - One of the best experts on this subject based on the ideXlab platform.

  • cross reactivity among edible nuts double immunodiffusion crossed Immunoelectrophoresis and human specific ige serologic surveys
    Annals of Allergy Asthma & Immunology, 2005
    Co-Authors: David W Goetz, B Whisman, Andrew D Goetz
    Abstract:

    Background As many as one third of all food allergen anaphylactic events are related to tree nut ingestion. Although concurrent allergen sensitivity to tree nuts is common, cross-reactivity among nut antigens is less well defined. Objective To survey serologic cross-reactivities among 7 tree nuts (walnut, pecan, hazelnut, cashew, Brazil nut, pistachio, and almond) and peanut. Methods Human specific IgE enzyme-linked immunosorbent assay inhibition was used to identify nut allergen cross-reactivities. Single-nut rabbit antisera were used in double immunodiffusion, crossed-line Immunoelectrophoresis, and crossed Immunoelectrophoresis with intermediate gel studies of nut antigen cross-reactivity. Results Nut specific IgE enzyme-linked immunosorbent assay inhibition demonstrated no cross-reactivities between peanut and tree nuts. Among tree nuts, 2 groups with allergen cross-reactivity were defined: (1) walnut, pecan, and hazelnut and (2) hazelnut, cashew, Brazil nut, pistachio, and almond. Double immunodiffusion, crossed-line Immunoelectrophoresis, and crossed Immunoelectrophoresis with intermediate gel results supported the same groupings of cross-reactive tree nuts and identified several less prominent nut-nut antigen cross-reactivities between groups and with peanut. Conclusion With few exceptions (notably limited peanut cross-reactivity with pistachio and walnut), peanut antigens did not serologically cross-react with tree nuts. Walnut, pecan, and hazelnut form a group of strongly cross-reactive tree nuts. Hazelnut, cashew, Brazil nut, pistachio, and almond form a group of moderately cross-reactive tree nuts. Cross-reactivities between these groups are less pronounced (notably limited cross-reactivity of walnut and pecan with Brazil nut). The strongest cross-reactivities among tree nuts follow botanical family associations: (1) walnut and pecan in the family Juglandaceae and (2) cashew and pistachio in the family Anacardiaceae.

Claus Koch - One of the best experts on this subject based on the ideXlab platform.

  • immunoelectrophoretic characterization and cross reactivity of rochalimaea henselae rochalimaea quintana and afipia felis
    Apmis, 1994
    Co-Authors: Kraesten Engbaek, Claus Koch
    Abstract:

    : The soluble antigens of Rochalimaea henselae, Rochalimaea quintana and Afipia felis were characterized by crossed Immunoelectrophoresis using bacterial sonicates as antigens against pooled hyperimmune rabbit sera. A precipitin pattern was drawn for each bacterium and shown to be reproducible and stable even when normal or preimmune rabbit serum was incorporated in the intermediate gel. By this technique 56 antigens were identified from R. henselae, 49 from R. quintana, and 39 from A. felis. The serological cross-reaction between R. henselae, R. quintana and A. felis, and between these 3 bacteria and 32 pathogenic bacteria was analysed by rocket-line Immunoelectrophoresis, crossed-line Immunoelectrophoresis, and tandem-crossed electrophoresis. It was concluded that (i) 4-7 antigens distinguish R. henselae, R. quintana and A. felis from each other, (ii) both Gram-positive and Gram-negative bacteria cross-react with R. henselae, R. quintana and A. felis antisera, (iii) the cross-reacting antigens of Gram-negative bacteria have both precipitating and non-precipitating specificities, whereas Gram-positive bacteria have mainly non-precipitating specificities, (iv) the cross-reacting antigens are common to several species, and (v) fewer cross-reacting antigens are found in phylogenetically disparate species than in more closely related species.

Jørgen Nedergaard Larsen - One of the best experts on this subject based on the ideXlab platform.

  • Immunoelectrophoresis for the Characterization of Allergen Extracts.
    Methods in molecular biology (Clifton N.J.), 2019
    Co-Authors: Gitte Nordskov Hansen, Jørgen Nedergaard Larsen
    Abstract:

    Immunoelectrophoresis can be used for analysis of individual proteins in complex mixtures. The conditions involved in Immunoelectrophoresis are mild, avoiding the risk of denaturation, and it is possible to perform relative quantification of individual components. The fundamental disadvantage is the dependence on rabbit antisera as reagents. The usefulness of Immunoelectrophoresis in allergy research is greatly enhanced by the possibility of identification of allergens to which the individual in question has IgE.The common principle is characterized by two independent electrophoreses having direction of current perpendicular to each other, i.e., crossed Immunoelectrophoresis (CIE). This ultimately results in the formation of characteristic bell-shaped precipitates, each precipitate representing one antigen. There is a linear relationship between the amount of antigen and size of precipitate for a given antibody concentration for each precipitate and so relative quantification can be performed. The sensitivity and resolution power of CIE are very high and there are multiple variations of the technique, some of which will be illustrated in this chapter.

  • Immunoelectrophoresis for the Characterization of Allergen Extracts
    Methods in molecular medicine, 2008
    Co-Authors: Gitte Nordskov Hansen, Jørgen Nedergaard Larsen
    Abstract:

    Immunoelectrophoresis can be used for analysis of individual proteins in complex mixtures. The conditions involved in Immunoelectrophoresis are mild, avoiding the risk of denaturation, and it is possible to perform relative quantification of individual components. The principle disadvantage is the dependence on rabbit antisera as reagents. The usefulness of Immunoelectrophoresis in allergy research is greatly enhanced by the possibility of identification of allergens to which the individual in question has IgE. The common principle is characterized by two independent electrophoreses having direction of current perpendicular to each other, i.e., crossed Immunoelectrophoresis (CIE). This ultimately results in the formation of characteristic bell-shaped precipitates, each precipitate representing one antigen. There is a linear relationship between the amount of antigen and size of precipitate for a given antibody concentration for each precipitate and so relative quantification can be performed. The sensitivity and resolution power of CIE is very high and there are multiple variations of the technique, some of which will be illustrated in this chapter.