Biomedical subjects
D Green
Publications and source records attributed to D Green.
An affluent society's excuses for inequality: developmental, economic, and educational.
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What's the dif on your tax return?
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The no-knock tax audit: better know your rights.
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When your income stops--this insurance starts.
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Postdoctoral endodontic educaton: the role of research.
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The patients that got away.
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Neurologic examination of the elderly.
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New cure for headache found in old Greek manuscript.
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Thermal titration: application of calorimetry to the study of plasma coagulation.
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Hippocrates, Plato and neurology.
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Double canals in single roots.
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Influence of affect on exposure-frequency estimates.
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A study of the variable response of human platelets to collagen: relation to aspirin-induced inhibition of aggregation.
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A clinico-pathological study of some factors influencing survival in cancer of the oesophagus: a survey of ten years' experience.
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The role of fluorine i8 scanning in the detection of skeletal metastases in early breast cancer.
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Ultrastructure of ristocetin aggregated normal human platelets: tortuous boundaries and swollen granules.
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Hemoglobin Abraham Lincoln, beta32 (B14) leucine leads to proline. An unstable variant producing severe hemolytic disease.
An unstable hemoglobin variant was identified in a Negro woman with hemolytic anemia since infancy. A splenectomy had been performed when the patient was a child. The anemia was accompanied by erythrocyte inclusion bodies and excretion of darkly pigmented urine. Neither parent of the proposita demonstrated any hematologic abnormality, and it appeared that this hemoglobin variant arose as a new mutation. Erythrocyte survival in the patient was greatly reduced: the erythrocyte t(1/2) using radiochromium as a tag was 2.4 days, and a reticulocyte survival study performed after labeling the cells with L-[(14)C]leucine indicated a t(1/2) of 7.2 days. When stroma-free hemolysates were heated at 50 degrees C, 16-20% of the hemoglobin precipitated. The thermolability was prevented by the addition of hemin, carbon monoxide, or dithionite, suggesting an abnormality of heme binding. An increased rate of methemoglobin formation was also observed after incubation of erythrocytes at 37 degrees C. The abnormal hemoglobin could not be separated from hemoglobin A by electrophoresis or chromatography, but it was possible to isolate the variant beta-chain by precipitation with p-hydroxymercuribenzoate. Purification of the beta-chain by column chromatography followed by peptide mapping and amino acid analysis demonstrated a substitution of proline for beta32 leucine. It appears likely that a major effect of this substitution is a disruption of the normal orientation of the adjacent leucine residue at beta31 to impair heme stabilization.