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Biomedical subjects

B Mattiasson

Publications and source records attributed to B Mattiasson.

At least 163 records · Page 9Linked to original sources
PubMed1981

Use of an internal sample attenuator in radioimmunoassay. Assay of triiodothyronine (T3) using starch particles containing entrapped charcoal and bismuth oxide in combination with free antibodies.

A radioimmunoassay for triiodothyronine involving no separate washing or separation steps is described. By using an internal sample attenuator, bismuth oxide, co-immobilized with the sorbent, charcoal, for the non-bound fraction of T3, a system was designed in which a suspension of starch spheres containing the sorbent and the attenuator was added after the immunological reaction had taken place. The particles sedimented and the whole test tube was counted in a gamma-counter. The coefficient of correlation between the results obtained with the present method and those from conventional procedures was 0.993.

Adsorption↗
PubMed1981

Application of partition affinity ligand assay (PALA) in quick test for quantitation of Staphylococcus aureus bacterial cells.

A novel immunochemical method for the quantitation of bacterial cells is described. The method, which is based on separation of bound from free reactants in aqueous two-phase systems has been studied both as direct and competitive binding assays, with a system consisting of intact cells of Staphylococcus aureus and human immunoglobulin G molecules. To achieve high resolution, one of the reactants was modified so that the two reactants, the bacterial cells and the immunoglobulin molecules, occurred in different phases of the phase system. When binding takes place, the partition of one of the reactants is changed. The degree of change is then correlated to the amount of reactant present. Using this method, cell numbers in the region 10(5)-10(7) can be quantified. An assay takes 40-90 min.

Bacteriological Techniques↗
PubMed1981

Enzyme thermistor analysis of penicillin in standard solutions and in fermentation broth.

Immobilized penicillinase was applied in an enzyme thermistor for calorimetric analysis of samples containing penicillin G. Standard solutions as well as extracts from fermentation broth were analyzed. The enzyme was applied bound either to porous glass or, when dealing with crude preparations, to the inner surface of nylon tubing. In the fermentation system studied, high concentrations of penicillin were present, thus allowing dilution to reduce the influence of the composition of the medium on the analysis. The useful linear concentration range was from 0.1 to 100 mM. The coefficient of correlation between analytical results obtained with the present method and those from conventional assays was 0.997.

Journal Article↗
PubMed1980

Partition affinity ligand assay (PALA): radioimmunoassay of digoxin.

A new approach to radioimmunoassay is described. Thanks to the use of an aqueous two-phase system for separation of bound and free ligand, a convenient procedure has been developed where soluble antibodies may be used and separate washing steps are unnecessary. Assay of digoxin in serum using the Partition Affinity Ligand Assay (PALA), gave results which correlated closely (r = 0.979) with those obtained with conventional RIA-procedures.

Immune Sera↗
PubMed1980

Partition affinity ligand assay (PALA). A new approach to binding assays.

A two-phase partitioning technique was used to separate free from bound labelled ligand in a binding assay. Efficient separation was accomplished by modifying one of the reactants in such a way that it partitions preferentially to one of the two phases. The biospecific interactions between the lectin concanavalin A and various carbohydrates and glycoproteins were investigated in this model study.

Antigen-Antibody Reactions↗
PubMed1980

A study of structurally related binding properties of concanavalin A using differential scanning calorimetry.

Differential scanning calorimetry has been used to study the interactions between concanavalin A and different carbohydrates. It was found that the binding of carbohydrate to concanavalin A stabilizes the structure of the protein as judged by an increase in transition temperature of the lectin. Furthermore, the degree of stabilization is shown to be a function of the association constant for each sugar moiety. Interactions between concanavalin A and the glycoprotein horseradish peroxidase were also studied. On changing the molar ratio of peroxidase to concanavalin A from 0.1 to 16, an initial dramatic increase in the transition temperature for concanavalin A was observed, but at ratios above four the degree of stabilization decreased; no stabilization of peroxidase was found in molar ratios above one. Results are also presented on the importance of Mn2+ and Ca2+ for the stabilization of the concanavalin A structure and for its ability to bind carbohydrates. In the presence of Mn2+ ions alone, the lectin could not form the necessary conformation for binding the carbohydrate. However, with Ca2+ ions alone the lectin was able to bind the carbohydrate ligands, as judged by the shift in its transition temperature.

Calcium↗
PubMed1979

Use of an enzyme thermistor in continuous measurements and enzyme reactor control.

The enzyme thermistor measures the heat produced by the action of an immobilized enzyme on a substrate present in the sample. Its application in analysis of discrete samples, e.g., in clinical chemistry, is well documented, but it has not been used so far for continuous measurements. We decribe here the application of the enzyme thermistor for continuous monitoring and control of enzyme reactors. An enzyme thermistor filled with coimmobilized glucose oxidase and catalase was used to measure the amount of glucose in the outflow from a column reactor containing immobilized lactase acting on a lactose solution pumped through the reactor. The lactose conversion was kept on a constant level, irrespective of the actual enzymatic activity in the reactor, by regulating the flow through the reactor. The experiments were carried out with aqueous solutions of lactose as well as with whey from cow's milk.

Calorimetry↗
PubMed1979

Uptake and efflux of noradrenaline from platelets; a model system for neurogenic mechanisms in essential hypertension.

1. The rate (k) of initial efflux of noradrenaline from platelets was determined in 63 individuals. A highly significant correlation was found between diastolic blood pressure and efflux rate. 2. When platelets are incubated in buffers with various Na+ concentrations in the range 110-170 mmol/l a higher Na+ concentration will give a faster efflux of noradrenaline for each concentration tested. 3. The value for k was determined in 41 normotensive first-degree relatives of hypertensive individuals and 21 persons with no family history of hypertension. Efflux rate of noradrenaline was significantly higher in the relatives and within this group was a subgroup with very high k values.

Adult↗
PubMed1978

Thermometric enzyme linked immunosorbent assay in continuous flow system: optimization and evaluation using human serum albumin as a model system.

Thermometric enzyme-linked immunosorbent assay (TELISA) is described. After the procedure of optimization, human serum albumin was assayed using anti-human serum albumin bound to Sepharose CL 4-B in the enzyme thermistor unit and catalase as label on the free antigen. The model system was used for assays down to 10(-13)M and the preparation of immobilized antibodies was used repeatedly up to 100 times. Comparative studies of the TELISA technique with bromocresol green, immunoturbidimetric and rocket immunoelectrophoretic methods were carried out and showed that TELISA could be used as an alternative method.

Catalase↗
PubMed1978

Non-equilibrium enzyme immunoassay of gentamicin.

We describe a fast, accurate non-equilibrium enzyme immunoassay for serum gentamicin. With use of isokinetic conditions an assay takes a total of 12 min, including regeneration of the immunosorbent. The coefficient of correlation between the present method and conventional microbiological assays was 0.98.

Catalase↗
PubMed1977

Enzyme thermistor determination of glucose in serum using immobilized glucose oxidase.

An enzyme thermistor assay for serum glucose is described. The glucose present in the sample is reacted in a small column containing glucose oxidase immobilized to controlled pore glass (single thermistor device). The heat produced in the primary reaction is measured directly in the column without any need for coupling reactions. The useful linear range is 0.01-0.45 mM glucose, permitting 50-fold dilution of serum samples. Advantages are low enzyme cost, due to the immobilization, insensitivity for the color or any turbidity of the sample, and no requirement for coenzyme or any ancillary reaction. Improved sensitivity and extended linear range (0.01--0.9 mM) can be attained through a secondary reaction using catalase. The application to glucose analysis of a split-flow enzyme thermistor equipped with a reference column to eliminate unspecific heat effects is also described. The enzyme thermistor determinations were also compared with a spectrophotometric continuous flow technique using a small column with immobilized glucose oxidase and 4-aminoantipyrine and phenol as color reagents.

Blood Glucose↗
PubMed1977

Aspects of microenvironmental compartmentation. An evaluation of the influence of restricted diffusion, exclusion effects, and enzyme proximity on the overall efficiency of the sequential two-enzyme system malate dehydrogenase--citrate synthase in its soluble and immobilized form.

Soluble bifunctional enzyme aggregates have been prepared by cross-linking the sequential enzymes malate dehydrogenase (EC 1.1.1.37) and citrate synthase (EC 4.1.3.7) using glutaraldehyde. The kinetic behaviour of this two-enzyme system in its aggregated and non-aggregated form was studied both in free solution and immobilized on Sepharose beads. This study was undertaken in order to distinguish between the following two factors which may account for the increased efficiency found in general in co-immobilized consecutive two-enzyme systems: (a) closer proximity between the participating enzymes and (b) establishment of a favourable microenvironment (such as higher local intermediate concentration caused by increased diffusional hindrance in the gel phase). It was found that in spite of a reduction of the distance between the two enzymes in the aggregated form by an estimated factor of 10(3), no kinetic advantage (shorter lag phase or higher steady-state rate) could be detected compared to the corresponding system with the two enzymes not linked to each other. However, both systems immobilized to Sepharose reached the steady-state rate of citrate formation almost immediately, in contrast to the corresponding free systems which exhibited pronounced lag phase. These results indicate that, at least in the above systems and under the conditions given, diffusional hindrance in the gel phase of the intermediate oxaloacetate, which is present in rate-limiting concentrations, is the dominant cause of the observed higher efficiency in immobilized systems.

Citrate (si)-Synthase↗