Crown immunity. Untouched by law.
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Biomedical subjects
Publications and source records attributed to C Campbell.
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Serum C-reactive protein determinations were performed on well and sick neonates, in order to gain information about normal values and its value in the diagnosis of neonatal septicaemia. The median value in 48 cord sera was 200 micrograms/l (range 15 to greater than 6,000 micrograms/L); there was no correlation between paired maternal and cord serum CRP levels (12 pairs). Thirty-six children were followed from birth for a mean of 20 days. There were 21 episodes of confirmed infection in 16 children, each associated with a sustained rise in C-reactive protein, often commencing before there was clinical evidence of infection. In four patients with raised levels, infection was suspected, but no firm evidence was obtained. In the remaining 16 children there were no values above 10 mg/l, and the 95th centile was about 6 mg/l, with no difference between values obtained in the first three days of life and those found subsequently. Hyaline membrane disease and jaundice were not associated with a rise. Raised serum C-reactive proteins is a good indicator of the presence of infection in the neonatal period.
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Cardiac tamponade is an important complication after cardiac surgery, yet little has been published on the echocardiographic diagnosis of this situation. The two-dimensional echocardiograms of 11 patients who required surgical relief of cardiac tamponade complicating cardiac surgery were therefore reviewed. Four had nonloculated pericardial effusions surrounding both ventricles. The other seven patients had a loculated posterior pericardial effusion; in three of these the effusion altered left ventricular posterior wall contour so that it was concave toward the effusion in the long-axis view; in two, a strikingly abnormal motion of the left ventricular posterior wall was noted, such that the width of the posterior pericardial space diminished in systole and widened abruptly in early diastole. The quantity of pericardial contents (fluid, blood or clot) evacuated surgically was smaller than usually encountered in patients with tamponade due to various "medical" conditions. Thus, unlike tamponade with other pericardial effusions, tamponade after cardiac surgery is due to a pericardial effusion that is smaller in volume, often loculated posteriorly and associated with certain unique two-dimensional echocardiographic features.
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A biochemical basis for the LEC10 mutant phenotype of Chinese hamster ovary cells has been identified. Independent LEC10 mutants, originally selected for resistance to the toxicity of ricin, have been shown to exhibit reduced binding of 125I-ricin at the cell surface. Although this is indicative of structural changes in cell-surface carbohydrates, labeling of plasma membranes with galactose oxidase/[3H]borohydride revealed no significant differences between mutant and parental cells. Alterations in the carbohydrates synthesized by LEC10 cells were, however, resolved by lectin-affinity chromatography of glycopeptides from the G glycoprotein of vesicular stomatitis virus (VSV) grown in LEC10. LEC10/VSV glycopeptides contain a fraction which is not bound to concanavalin A-Sepharose but is strongly retarded on E-PHA (erythroagglutinin from Proteus vulgaris)-agarose. In contrast, CHO/VSV glycopeptides or those from a LEC 10 revertant (R.LEC 10/VSV) do not contain carbohydrates with these properties. High-field 1H NMR spectroscopy of the novel LEC10/VSV carbohydrates showed that they are complex, biantennary structures containing N-acetylglucosamine in beta(1,4)-linkage to the beta-linked core mannose residue. The presence of these structures correlates with the expression of the enzyme responsible for the addition of this "bisecting" GlcNAc residue, UDP-GlcNAc:glycopeptide beta-4-N-acetylglucosaminyltransferase III (GlcNAc-TIII). Parental Chinese hamster ovary cells and the LEC10 revertant possess no detectable GlcNAc-TIII activity. The combined evidence suggests that the LEC10 mutation induces the expression of the GlcNAc-TIII enzyme in Chinese hamster ovary cells.