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E F Osserman

Publications and source records attributed to E F Osserman.

69 records · Page 4Linked to original sources

Crystallization of human lysozyme.

Lysozyme, isolated from the urine of patients with monocytic leu kemia, has been crystallized as the chlo ride at pH 4.5 and at pH 10.5. The crystal forms of the human enzyme show certain similarities as well as dis tinct dissimilarities compared with the crystal forms of lysozyme chloride from hen's egg white.

Crystallization↗

Serum and urinary lysozyme (muramidase) in monocytic and monomyelocytic leukemia.

Markedly increased quantities of lysozyme have been found in the serum and urine (ranging to 2.6 g per day) of ten consecutive cases of monocytic and monomyelocytic leukemia. The enzyme has been isolated from the urine of several cases and physicochemically and immunochemically characterized. It is apparently identical to the lysozyme of normal tears, saliva, leukocytes, and serum, but structurally different from the lysozyme of hen's egg white. The activity of the human enzyme assayed with M. lysodeikticus organisms is 3 to 12 times greater than egg white lysozyme at equivalent concentrations. An agar plate method has been developed for quantitating lysozyme activity in small samples (approximately 25 microl) of serum, urine, or other biological fluids. The range and reproducibility of this method were found to be superior to previously available lysozyme assay procedures. Present evidence indicates that lysozyme is the principal, if not the sole, product of the proliferating monocytes in monocytic and monomyelocytic leukemia, and quantitation of serum and urine lysozyme should be a useful diagnostic procedure for these leukemias.

Aged↗

Notation for human immunogobulin subclasses.

After consultation between immunologists from a number of countries a nomenclature for human immunoglobulins was proposed in 1964 and was published in the Bulletin of the World Health Organization.(1) However, that proposed scheme of notation, which has already gained wide acceptance, left several specialized areas of nomenclature still to be resolved; one of these was the subclasses of immunoglobulins. Some of the research workers most closely concerned with the problem have now agreed upon a unified scheme for the notation of the human immunoglobulin subclasses, and, in particular, of the immunoglobulin G subclass, for which two different nomenclatorial schemes have been followed in recent years. Their proposals are given below.

Humans↗

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↗