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Biomedical subjects

M L Beck

Publications and source records attributed to M L Beck.

At least 73 records · Page 4Linked to original sources
PubMed1977

RH nomenclature.

Explore the source record for details and available documents.

Rh-Hr Blood-Group System↗
PubMed1975

A serum haemagglutinating property dependent upon polycarboxyl groups.

A serum agglutinin reactive with red cells in the presence of polycarboxyl groups is reported. It is likely that this represents an additional example of the type of agglutinin previously described as agglutinating red cells in the absence of ionized calcium. Experimental evidence is presented indicating that it is free polycarboxyl groups that potentiate agglutination and that any metal ion, such as calcium, capable of chelating with these groups will prove to be inhibitory.

ABO Blood-Group System↗
PubMedDate not supplied

Differential reactivity of cardiac and skeletal muscle from various species in two generations of cardiac troponin-T immunoassays.

Cardiac troponin T (cTnT) is being increasingly used as a blood marker of acute or ongoing cardiac injury in various laboratory animals although the range of species in which it is applicable and its tissue selectivity has not been demonstrated. To address this concern, cardiac and skeletal muscle biopsy specimens from various species were homogenised and diluted, and their reactivity was then determined in the first- and second-generation immunoassays for cTnT. Cardiac tissue reactivity was found for all species studies, being highest for rats and several-fold lower for chickens and fish, and intermediate for dogs, pigs, goats, cows, sheep, horses, rabbits, and turkeys. Skeletal muscle had 10 per cent of the reactivity of cardiac muscle in the first-generation assay and 1 per cent of the reactivity of cardiac muscle in the second-generation assay. In the absence of moderate to marked skeletal muscle injury, the second-generation cTnT immunoassay has sufficient reactivity and tissue-selectivity to serve as a blood test for the discrimination between cardiac and skeletal muscle injury in a wide range of species.

Animals↗
PubMedDate not supplied

Unexpected limitations in the use of commercial antiglobulin reagents.

The majority of antiglobulin sera used in blood banks in the USA are commercially prepared immune rabbit sera, designed to be reactive only with human red blood cells sensitized with immunoglobulins or complement components. Current manufacturing methods result in a product that gives reliable specific reactions provided that the test red blood cells are normal, particularly with respect to sialic acid levels. This report describes our findings of false positive antiglobulin tests caused by incompletely absorbed antiglobulin reagents when cells with low sialic acid levels were tested. An evaluation of nine commercially prepared antiglobulin reagents revealed, in many of them, the presence of anti-species antibody, anti-T, and anti-Tn. Blood bank personnel must be aware of these characteristics especially when testing either enzyme premodified or polyagglutinable cells. The use of incompletely absorbed reagents might account for positive direct antiglobulin tests that are encountered occasionally in apparently normal healthy individuals. Furthermore, recent protocols advocating the use of trypsinized cells for the evaluation of anti-C3d activity of antiglobulin sera are invalid if the reagent is inadequately absorbed of anti-species agglutinins.

Agglutinins↗
PubMedDate not supplied

Serologic activity of fatty acid dependent antibodies in albumin-free systems.

Fatty acid dependent agglutinin (FADA) refers to serum with the special ability to cause agglutination of red blood cells in the presence of certain fatty acids. The agglutinating mechanism is unclear. It has been proposed that the agglutinin reacts with albumin that has been conformationally altered by sodium caprylate and that the immune complex is passively adsorbed onto red blood cells. This report presents data that contradicts the proposal assigning a specific role to albumin in the agglutinating mechanism. FADA were isolated by column chromatography of resolubilized euglobulin preparations. No evidence of contamination with albumin was obtained in those IgM fractions possessing FADA activity. We propose, as an alternative explanation, that the serologic activity of FADA depends upon the interaction of IgM agglutinins with haptenic fatty acids.

Antibody Specificity↗
PubMedDate not supplied

Coexistent Tk and VA polyagglutinability.

Serologic investigations of the red blood cells of two patients indicated polyagglutination as the cause of compatibility problems. Lectin studies to classify the variety of polyagglutination demonstrated the simultaneous exposure of two latent membrane receptors, Tk and VA. It is proposed that different bacterial enzymes were responsible.

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