Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several cytochemical characteristics of mononuclear phagocytes which are used as identifying markers were studied in reactive microglia from traumatically damaged brain tissue of guinea pigs and humans as well as in globoid cells from a child with familial globoid cell leukodystrophy (Krabbes' disease). The following cytochemical methods were used: acid phosphatase, lysozyme, peroxidase, alpha-naphthyl acetate esterase, alpha-naphthyl butyrate esterase, adenosine triphosphatase, and the periodic acid-Schiff reaction (PAS reaction). Distinct activity of almost all enzymes and the PAS reaction were demonstrable in reactive microglia and globoid cells. Peroxidase however could not be demonstrated in globoid cells. The similarity of the cytochemical characteristics for mononuclear phagocytes, reactive microglia, and globoid cells tends to indicate a common identity for these cell types. The lack of peroxidase in globoid cells may be due to a final maturation and differentiation after the monocyte stage.
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PMID:Cytochemical markers for mononuclear phagocytes as demonstrated in reactive microglia and globoid cells. 677 84

A histochemical study of the enzyme profile of Krabbe's cells revealed a high activity of lysosomal enzymes, including the tartrate-resistant isoenzyme of acid phosphatase, and considerable activity of extralysosomal nonspecific esterase and mitochondrial and extramitochondrial dehydrogenases. The presence of lysozyme was demonstrated. This generally high metabolic activity was found closely reminiscent of that in Gaucher's cells and in epitheloid transformed macrophages though quite unlike the exclusive predominance of lysosomal enzyme activity typical of classical foamy storage cells in Niemann-Pick and Wolman's disease.
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PMID:A histochemical study of the enzyme profile of Krabbe's cells. 688 Jun 19

We constructed a plasmid that directs the synthesis and secretion of hepatitis B virus (HBV) surface antigen (HBsAg) particles by Saccharomyces cerevisiae. This plasmid contains a proteinase-resistant HBsAg M (M-P31c) gene fused at its 5'-terminus with a chicken-lysozyme signal peptide (C-SIG) gene, which is placed under the yeast GLD (glyceraldehyde-3-phosphate dehydrogenase gene) promoter. The products encoded by the "C-SIG+M-P31c" (LM-P31c) gene were synthesized and assembled themselves into HBsAg particles in yeast cells, and the particles were released into the medium along with poly-HSA (polymerized human serum albumin) binding activity. The HBsAg particles purified from the medium were very similar in density (1.19 g cm-3), size (19.2 +/- 0.8 nm in diameter) and shape (sphere) to human-plasma-derived HBsAg particles. When several sec (temperature-sensitive secretion-defective) mutants were used as host cells, the release of HBsAg particles into the medium was blocked at 37 degrees C but not at 25 degrees C, indicating that the HBsAg particles are exported through the normal yeast secretion pathway. To our knowledge, this is the first report that yeast cells are capable of secreting particles into the medium.
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PMID:Saccharomyces cerevisiae can release hepatitis B virus surface antigen (HBsAg) particles into the medium by its secretory apparatus. 776 88