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R Maiolini

Publications and source records attributed to R Maiolini.

25 records · Page 2Linked to original sources
PubMed1980

[Enzymo-immunologic determination of the class of antiglobulin factors].

The authors describe an enzymo-immunologic method of determination of the class of rheumatoid factors (RF). This technic includes 3 main stages : 1) extraction of RF by fixation on aggregated rabbit IgG previously adsorbed on the walls of a plastic tube; 2) recognition of RF linked to the solid phase by anti-IgG addition, and addition of human IgA and IgM linked to glucose oxidase; 3) revelation of the enzyme activity linked to the solid phase : this enzyme activity directly depends on the levels of RF to be estimated. The results are expressed as a percentage of the fixation of a reference serum obtained from a patient with rheumatoid arthritis (RA). This serum presents an antiglobulin activity in the 3 major classes of immunoglobulins. The coefficients of variation of intra- and intersystem reproductibility lay between 5,6 and 17.8%. The specificity of the estimation was controlled by the localisation of the antiglobulin activity of the sera after chromatography on Sephadex G200 and by estimation of RF after their absorption by an aggregated IgG immunoadsorbant. This technic was applied to the identification of RF in RA (90 cases); in diseases not related to RA and in control subjects : the sensitivity of this method appears greater than that of technics previously described (immuno-fluorescence, Rose-Waaler reaction) in fact, only 12,2% of sera of patients with RA remain negative with this new test. However, this greater sensitivity does not seem to have altered the clinical specificity of the test : in fact, only 8,4% of the sera of patients with diseases unrelated to RA are positive by this method, which, moreover, may be explained by the age of these subjects (average age 71.5 years).

Aged↗
PubMed1979

Coupling of gamma-globulin to microcrytstalline cellulose by periodate oxidation.

Anti-rabbit IgG sheep gamma-globulins were covalently coupled to periodate oxidized microcrystalline cellulose using the Schiff reaction. Optimal conditions (sodium m-periodate concentration and gamma-globulin amount) were studied measuring the ability of this solid-phase antibody to bind glucose oxidase-labeled rabbit IgG.

Animals↗
PubMed1978

A sandwich method of enzyme-immunoassay. II. Quantification of rheumatoid factor.

A sandwich enzyme-immunoassay (EIA) has been applied to the determination of the rheumatoid factor (RF). This non-competeitive assay comprises 3 steps: 1) the RF to be assayed is extracted for the biological medium by an immunosorbent of aggregated IgG linked to cellulose; 2) the solid phase is then incubated with the enzyme-labeled aggregated IgG; 3) the enzymatic activity of the immunosorbent is then measured with a suitable chromogenic reagent. This activity is a direct function of the amount of RF to be assayed. This assay gave reproducible results in the range 0.5-50.0 IU/ml. A good agreement was obtained between the EIA and the Waaler-Rose test but no correlation was obtained with the latex slide-test. This assay permits a quantitation of RF with a good reproducibility (coefficient of variation in the range of 10% for moderately elevated values) and thus allows a closer follow-up of patients. The results do not depend on the interpretation of the technician performing the test, which can be easily automated. Finally, it may detect some RF devoid of agglutinating activity.

Animals↗
PubMed1975

Enzymoimmunoassay of human alpha-fetoprotein.

A non-competitive method for the determination of human alpha-fetoprotein (AFP) in serum, using a pure specific antibody linked to glucose oxidase is described. When applied to human AFP, this method gives reproducible results in the range 0.7 to 15 ng/ml, in a relatively short time (6 hr). AFP sera levels of healthy human adults, pregnant women and adults with liver diseases, were tested both by enzymoimmunoassay and radioimmunoassay. In all cases, good agreement was noted between the two methods.

Adsorption↗
PubMed1975

A sandwich method of enzymoimmunoassay. I. Application to rat and human alpha-fetoprotein.

An enzymoimmunoassay (EIA) for the quantitation of soluble antigens having at least two antibody-combining sites is descirbed. This non-competitive sandwich method comprises three steps: 1) the antigen to be assayed is reacted with the antibody-coated cellulose immunosorbent, 2) the enzyme-labelled antibody is then incubated with the antigen bound to the solid phase, 3) the enzymatic activity of the immunosorbent is then measured. This activity increases with the quantity of antigen to be assayed. Examples of the application of this method to the assay of rat and human alpha-fetoprotein (AFP) are given. When applied to rat and human AFP, this assay gives reproducible results in the range of 10--1000 ng/ml and 3-1000 ng/ml respectively. AFP sera concentrations of normal and pregnant rats were assayed by EIA, radioimmunoassay RIA and rocket-immunoelectrophoresis (RIE). In all the cases good agreement was noted among these three techniques. Rheumatoid factor, whenever present, may interfere with the assay. However, the effect of this interaction can be eliminated. The advantages of the EIA method can be listed as follows: a) no pure antigen is required, b) the final color reaction is developed from the solid phase. This feature eliminates most non-specifically interfering factors, c) the range of the assay covers a 2 log-scale, d) only inexpensive equipment is used, e) results are obtained within 24 hr, f) sensitivity and reproducibility lie within a range comparable to that of RIA.

Animals↗