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Biomedical subjects

M Wagstaff

Publications and source records attributed to M Wagstaff.

32 records · Page 2Linked to original sources
PubMed1980

An anaesthetic scavenging system for paediatric and adult use.

A scavening dish is described which removes large volumes of contaminated air. It can be placed close to the open-tailed bag of the paediatric T piece to provide a safe, convenient and efficient scavenger without any modification of the patient circuit. Measurements before and after installation have shown it to be capable of reducing nitrous oxide levels in the operating theatre to between 40 and 0 parts per million. The dish has been incoporated into a scavening system which can also be used with a standard antipollution valve or ventilator exhaust port.

Adult↗
PubMed1980

Biochemical and immunological characterization of ferritin from leukaemic cells.

Ferritin was prepared from the leucocytes of four patients with acute myeloblastic leukaemia (AML) and eight patients with chronic myeloid leukaemia (CML). Isoelectric focusing demonstrated a prominent relatively basic band in all the CML cell ferritins. The iron content of all the ferritins was very low (max 180 atom/molecule). Thus there was little evidence for the role of leucocyte ferritin as an iron store or for iron as the major factor responsible for the initiation of ferritin synthesis. The iron uptake properties, subunit analyses, immunological reactivities and other immunological studies indicated that leukaemic cell ferritins had similar properties to tissue ferritins.

Acute Disease↗
PubMed1979

Binding of human serum ferritin to concanavalin A.

1. A high proportion of the ferritin in normal serum binds to concanavalin A. Binding is prevented by the addition of alpha-D-methylglucoside to the reaction mixture. 2. Ferritin in extracts of normal heart, liver and spleen or serum ferritin from patients with massive hepatic necrosis does not bind to concanavalin A. 3. Isoelectric focusing of preparations of serum ferritin from patients with primary haemochromatosis shows that the ferritin fraction binding to concanavalin A consists, predominantly, of the more acidic isoferritins. 4. These findings suggest that carbohydrate residues may be added to ferritin during its secretion into the plasma. Glycosylation may account for the heterogeneity of serum ferritin on isoelectric focusing. 5. Direct release of intracellular ferritin from damaged tissue may be indicated by an increase in the proportion of circulating ferritin which does not bind to concanavalin A. Such an increase has been found in sera from patients with iron overload.

Concanavalin A↗
PubMed1978

Properties of human tissue isoferritins.

1. Human liver ferritin was separated by preparative isoelectric focusing into six fractions. 2. Except for the least acidic fraction the reactivity with antibody against spleen ferritin increased with rising pI, but with antibody against heart ferritin the reactivity decreased. 3. The highest iron content was found in the most acidic isoferritins and progressively decreased with rising pI. 4. Iron uptake was studied in apoferritin prepared from heart and liver ferritin fractions separated by ion-exchange chromatography. There was good correlation between the rate of iron uptake and pI. The most acidic fractions took up iron more rapidly than did the more basic ones. 5. Ferritin was prepared from heart, liver, spleen and kidney. There was little difference on isoelectric focusing between ferritin obtained from normal tissues and the corresponding iron-loaded tissues from patients who had received multiple blood transfusions. The iron-loaked heart ferritin invariably contained relatively more of the basic isoferritins. Normal and iron-overloaded heart ferritins were separated into isoferritin fractions by ion-exchange chromatography, and in each case there was a fall in iron content as the pI increased. The iron content of ferritin from the iron-overloaded heart was higher throughout than that from normal heart. 6. There is a relationship between the rate of iron uptake by apoferritin and pI, and this probably accounts for the variation in iron content of the isoferritins found in human liver and heart.

Apoferritins↗
PubMed1977

Isoferritins in acute leukaemia.

Leucocytes containing a high proportion of blast cells were obtained from 11 patients with acute myeloid leukaemia, and leucocytes were also obtained from 2 normal subjects. Ferritin was partially purified from leucocyte extracts and subjected to anion-exchange chromatography and isoelectric focusing. The Fe content of leucocyte ferritin was low, and in all but one case the preparations contained isoferritins corresponding to those found in normal tissues or serum. Only some of the preparations contained the relatively acidic isoferritins which have been described as "carcinofoetal", but which are also present in normal heart and kidney. Ferritin from one patient contained isoferritins of lower isoelectric point than heart ferritin. These results show that there does not appear to be any specific isoelectric focusing pattern for leukaemic cells, and that assays for acidic isoferritins are unlikely to be of use in the diagnosis of leukaemia and in monitoring treatment. However, the very acidic protein found in one preparation suggests that the search for abnormal subunits of ferritin may be fruitful in acute leukaemia.

Chromatography, Ion Exchange↗
PubMed1976

The purification and properties of ferritin from human serum.

1. Ferritin has been isolated from the serum of four patients with iron overload by using two methods. 2. In method A, the serum was adjusted to pH 4.8 and heated to 70 degrees C. After removal of denatured protein, ferritin was concentrated and further purified by ion-exchange chromatography and gel filtration. In most cases, only a partial purification was achieved. 3. In method B, ferritin was extracted from the serum with a column of immuno-adsorbent [anti-(human ferritin)] and released from the column with 3M-KSCN. Further purification was achieved by anion-exchange chromatography followed by the removal of remaining contaminating serum proteins by means of a second immunoadsorbent. Purifications of up to 31 000-fold were achieved, and the homogeneity of the final preparations was demonstrated by polyacrylamide-gel electrophoresis. 4. Serum ferritin purified by either method has the same elution volume as human spleen ferritin on gel filtration on Sephadex G-200. Serum ferritin has a relatively low iron content and iron/protein ratios of 0.023 and 0.067 (mug of Fe/mug of protein) were found in two pure preparations. On anion-exchange chromatography serum ferritin has a low affinity for the column when compared with various tissue ferritins. Isoelectric focusing has demonstrated the presence of a high proportion of isoferritins of relatively high pI. 5. Possible mechanisms for the release of ferritin into the circulation are briefly discussed.

Chromatography, Ion Exchange↗