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)

Intracellular lysozyme concentration was measured in neutrophilic granulocytes from 25 patients with multiple myeloma. At diagnosis intraneutrophil lysozyme activity was significantly reduced (mean reduction 50%). During clinical remission after 1-4 months of intensive chemotherapy values were normalized. In 18 cases studied at various stages of the disease from 6 to 70 months after diagnosis there was a significant negative correlation between the duration of the disease and neutrophil lysozyme concentration. The decrease in neutrophil lysozyme concentration was significantly correlated to clinical disease activity and the percentage of plasma cells in bone marrow aspirates, whereas there was no correlation between the concentration of M-protein in serum and the neutrophil lysozyme concentration. Plasma lysozyme concentration was normal. In contrast, neutrophil lysozyme concentration was normal in 18 patients with stage III-IV malignant lymphoma. Plasma lysozyme in this group was significantly higher than normal. The difference in neutrophil lysozyme patterns between multiple myeloma and malignant lymphoma supports the hypothesis that the defect in neutrophil maturation seen in malignant blood disorders is directly related to the infiltration of the bone marrow by pathologic cells.
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PMID:Neutrophil defect in multiple myeloma. Studies on intraneutrophilic lysozyme in multiple myeloma and malignant lymphoma. 95 76

The study of the kinetic curves of the lysis of group A S. pyogenes cell-walls (cells), serovars 29 and 12 M, variants M+ and M-; with endo-N-acetyl-muramidase revealed that the kinetics of the lysis of virulent and avirulent strains was different: variant M- was lyzed faster than M+. This difference in the cell-wall lysis of both variants made it possible to use this method for the identification of M+ and M- states of the strains. 18 group A S. pyogenes cultures were studied. The cultures isolated from healthy and sick children in an organized group belonged to variants both M+ and M-. The pepsin fragments of M-proteins of group A S. pyogenes, type M 1, isolated in dynamics from a carrier and a patient, were studied. Their amino acid compositions were studied, and differences between them were established. The data thus obtained indicate that heterogeneity is characteristic of both the surface structure of streptococci and the individual components of their surface, in particular, M-protein.
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PMID:[The M-protein heterogeneity of Streptococcus pyogenes strains isolated from clinically healthy and ill children in an organized collective]. 765 28

Streptococcus pyogenes adheres to human epithelial cells in vitro and in vivo. To identify adhesins, cell wall components were extracted from S. pyogenes M6 with alkali or by treatment with mutanolysin and lysozyme. HEp-2 cells were incubated with extracts of S. pyogenes M6 and then analyzed by Western blot (immunoblot) assays, using antibodies to S. pyogenes. Only one streptococcal component (62 kDa) was bound to HEp-2 cells and was identified serologically as M6 protein. Experiments with pepsin-cleaved fragments of M protein indicated that the binding site was located at the N-terminal half of the molecule. M protein was bound selectively to two trypsin-sensitive surface components, 97 and 205 kDa, of HEp-2 cells on nitrocellulose blots of sodium dodecyl sulfate-polyacrylamide gels. Tritium-labeled lipoteichoic acid bound to different HEp-2 cell components, 34 and 35 kDa, in a parallel experiment, indicating that lipoteichoic acid was not complexed with M protein and does not mediate M-protein binding. The four HEp-2 components were unrelated to fibronectin since they did not react with specific antibodies. An M-protein-deficient (M-) strain of streptococcus (JRS75), grown in chemically defined medium, showed 73% less adhesion activity to HEp-2 monolayers than an M+ strain (JRS4). Streptococcal adhesion was insensitive to competitive inhibition by selected monosaccharides. These results indicate that M protein binds directly to certain HEp-2 cell membrane components and mediates streptococcal adhesion.
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PMID:M protein mediates streptococcal adhesion to HEp-2 cells. 830 Feb 5