Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cellular localization of enzymes in Diplococcus pneumoniae was examined by fractionation of spheroplasts. A deoxyribonuclease implicated in the entry of deoxyribonucleic acid (DNA) into the cell during genetic transformation was located in the cell membrane. This enzyme, the major endonuclease of the cell (endonuclease I), which is necessary for the conversion of donor DNA to single strands inside the cell and oligonucleotides outside, thus could act at the cell surface. Another enzyme, the cell wall lysin (autolysin), was also found in the membrane fraction. Other enzymes, including amylomaltase, two exonucleases, and adenosine triphosphate-dependent deoxyribonuclease, and a restriction type endonuclease, were located in the cytosol within the cell. None of the enzymes examined were predominantly periplasmic in location. Spheroplasts were obtained spontaneously on incubation of pneumococcal cells in concentrated sugar solutions. The autolytic enzyme appears to be involved in this process. Cells that were physiologically competent to take up DNA formed osmotically sensitive spheroplasts two to three times faster than cells that were not in the competent state. Although some genetically incompetent mutants also formed spheroplasts more slowly, other such mutants formed them at the faster rate.
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PMID:Membrane location of a deoxyribonuclease implicated in the genetic transformation of Diplococcus pneumoniae. 0 Mar 66

Patients diagnosed as suffering from erysipelas or cellulitis were subjected to bacteriological and serological investigations. The serological tests used included the anti-streptolysin O reaction (ASO), the anti-deoxyribonuclease B test (ADB) and the anti-hyaluronidase tests (AHT) that are specific both for the group A streptococcus (Streptococcus pyogenes) and for the human pyogenic streptococci of group C or group G. Antibody tests to the alpha-lysin and the nuclease of Staphylococcus aureus were also employed. Conventional bacteriological culture methods were used plus needle aspiration of injected saline in most patients with erysipelas, but recognized pathogens were isolated in only 42% of cases. Our results indicate the limitations of these tests for making initial diagnoses and deciding treatment. Serial serological testing was very successful in differentiating cellulitis due to group A, C or G haemolytic streptococci, or occasionally Staphylococcus aureus, but was positive in only 40% of cases of erysipelas.
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PMID:The value of bacteriology and serology in the diagnosis of cellulitis and erysipelas. 400 55

The sensitivity of Streptococcus faecalis (ATTC 8043) to S. zymogenes X-14 bacteriocin depends greatly on its physiological age. Sensitivity decreases from the mid-log phase on and is completely lost in the stationary phase. The sensitivity of erythrocytes to the hemolytic capacity of the bacteriocin showed considerable species variation. The order of increasing sensitivity was goose < sheep < dog < horse < human < rabbit. However, when red cell stromata were used as inhibitors of hemolysis in a standard system employing rabbit erythrocytes the order of increasing effectiveness was sheep < rabbit < human < horse < goose. When rabbit cells were used in varying concentrations with a constant hemolysin concentration, there was a lag of about 30 min, which for a given hemolysin preparation was constant for all red cell concentrations. Furthermore, the rate of hemolysis increased with increasing red cell concentration. If red cells are held constant and lysin varied, the time to reach half-maximal lysis varies directly with lysin but is not strictly proportional. Bacterial membranes were one to three orders of magnitude more effective than red cell stromata as inhibitors. The order of increasing effectiveness seems to be Escherichia coli < Bacillus megaterium < S. faecalis < Micrococcus lysodeikticus. In addition to membranes, a d-alanine containing glycerol teichoic acid, trypsin in high concentration, and deoxyribonuclease also inhibited hemolysis. Ribonuclease, d-alanine, l-alanine, dl-alanyl-dl-alanine, N-acetyl-d-alanine, N-acetyl-l-alanine did not inhibit hemolysis.
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PMID:Bacteriocin (hemolysin) of Streptococcus zymogenes. 497 10