[A new risk in the occupational medicine setting: mobbing].
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Humans↗
Biomedical subjects
M Adinolfi
Publications and source records attributed to M Adinolfi.
Human lysozyme (origin and distribution in health and disease).
Histochemical and in particular immunoperoxidase techniques have extended our knowledge about the cellular distribution of LZM. The enzyme has been detected in: 1. granulocytes, which synthesize LZM in bone marrow; 2. cells of the mononuclear phagocytic system, which synthesize LZM continuously; 3. various exocrine glands, whose LZM is probably in part synthesized locally and in part derived from blood; 4. cartilage, which probably synthesizes LZM and 5. the kidney, in which LZM is serum-derived. In pathological conditions, such as inflammation and neoplasia, most LZM-positive cells at the site of disease are either granulocytes or members of the mono-nuclear phagocytic system. A notable exception are the metaplastic Paneth cells that occur along the gastrointestinal tract in inflammation and neoplasia. LZM is an antibacterial agent, but evidence is accumulating which suggests that the enzyme might have other functions as well.
Animals↗
Primary prevention of inherited disorders. Present and future possibilities.
Two models are presented of active prevention of human inherited diseases. In the first case, prevention of neural tube defects in man and mouse is achieved by the administration of vitamin A or a vitamin complex. In the second instance, correction of lysosomal enzyme deficiencies, research is in progress to identify cells which produce the missing enzyme and cannot be acutely rejected once transplanted in affected patients. Both attempts are still surrounded by controversy and uncertainties and are based on empirical grounds since little is yet known about the cause of the defects at molecular level.
Amnion↗
Immunological reactivity of native and modified alcohol dehydrogenase (ADH).
The extent to which treatment of horse liver alcohol dehydrogenase (ADH) by procedures known to disturb the Zn association induced conformation changes detectable by immunological techniques has been investigated. Treatment of ADH by sodium dodecyl sulphate or by total reduction and carboxymethylation leads to complete loss of reactivity with a rabbit immune serum against the native enzyme. After selective carboxymethylation the enzymatic activity was reduced but the preparation had the same immunological activity of the native enzyme. Similar results were obtained when ADH was treated with reagents known to react with the "functional" Zn atoms, such as sodium dietyldithiocarbamate, 1,10 phenanthroline, and 2,2' bipyridine. In contrast dialysis in 0.01M phosphate buffer containing 0.1mM EDTA removing the "structural" Zn atoms leads to a parallel decrease of enzymatic and immunological activity. Thus loss of "structural" Zn atoms affects the immune reactivity of ADH differently from the loss of "functional" Zn atoms.
Alcohol Dehydrogenase↗