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

The ability of several cell wall fractions of Micropolyspora faeni, a thermophilic actinomycete associated with farmer's lung disease, to activate complement is reported. Cell walls, obtained by mechanical disruption, were purified by enzyme treatment and chemical extractions. Fractions containing the most purified cell walls were most active in consuming complement, as measured by reduction of hemolytic complement levels of normal human serum. Cell wall fractions activated the alternative complement pathway, as shown by monitoring the conversion of C3 proactivator (factor B) to C3 activator (activated factor B) in the presence of specific cation chelators. Selective degradation of cell walls by lysozyme resulted in a decreased ability to consume complement and implicated peptidoglycan as the major complement-reactive component. The role of this nonspecific complement activation in relation to farmer's lung disease is discussed.
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PMID:Complement activation by cell wall fractions of Micropolyspora faeni. 73 Mar 72

Pleural fluids from 10 patients with tuberculous pleural effusions contained high levels of small molecular weight breakdown products of C3 (C3d) and of properdin factor B (Ba) when compared to 16 patients with effusions of neoplastic origin (P less than 0.001). The same fluids exhibited overlapping values of haemolytic factor B, classical or alternative pathway-mediated haemolytic activity and native C3. A significant correlation between Ba and lysozyme levels was found in all effusions tested (P less than 0.05). These findings suggest that activation of the complement system is an important aspect of the extensive inflammation and tissue destruction characteristic of human tuberculosis.
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PMID:High levels of complement breakdown products in tuberculous pleural effusions. 660 98

Coaggregation occurred between Porphyromonas gingivalis and mutans streptococci. The coaggregation was completely inhibited by L-arginine, N alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK), and a trypsin inhibitor, and weakly inhibited by L-lysine, N-ethylmaleimide, lysozyme, and human whole saliva. The results of heat and proteinase K treatment suggested that a heat-labile proteinaceous substance of P. gingivalis and a heat-stable substance of mutans streptococci may play a role in the coaggregation. Mutans streptococci also aggregated in the presence of the heat-labile factor in the supernatant of P. gingivalis. The aggregation was also inhibited by L-arginine, TLCK, and a trypsin inhibitor.
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PMID:Coaggregation between Porphyromonas gingivalis and mutans streptococci. 796 75