93 research outputs found
Systemic lupus erythematosus and increased risk to develop B cell malignancies: Role of the p200-family proteins
No full textInterferon-inducible p200-family protein IFI16, an innate immune sensor for cytosolic and nuclear double-stranded DNA: Regulation of subcellular localization
No full textFactors affecting the synthesis and distribution of beta-lactamase in Mycobacterium smegmatis SN2 cultures
No full textA high level of extracellular beta-lactamase activity was detected in cultures ofMycobacterium smegmatis SN2. The extracellular distribution of the enzyme varied with growth conditions such as additional carbon source and pH of the medium. Addition of chloramphenicol tothe culture inhibited the increase in the extracellular beta-lactamase activity. Cell wall damage or autolysis may be responsible for the extracellular beta-lactamase activity
Characterization of beta-lactamase from Mycobacterium smegmatis SN2
No full textbeta-Lactamase from Mycobacterium smegmatis SN2 was purified to homogeneity. The molecular weight of the enzyme was 30,000 and the isoelectric point was 4.1. The enzyme showed maximal activity at pH 6.5 and 56~ and resembled the plasmid-mediated TEM-type beta-lactamases commonly encountered in gram-negative bacteria in substrate profile. The enzyme shared antigenic structure with beta-1actamase from Mycobacterium butyricum ATCC 19979 and Escherichia coli HB101 (pBR322)
Factors affecting the synthesis and distribution of β-lactamase in Mycobacterium smegmatis SN2 cultures
No full textA high level of extracellular β-lactamase activity was detected in cultures of Mycobacterium smegmatis SN2. The extracellular distribution of the enzyme varied with growth conditions such as additional carbon source and pH of the medium. Addition of chloramphenicol tothe culture inhibited the increase in the extracellular β-lactamase activity. Cell wall damage or autolysis may be responsible for the extracellular β-lactamase activity
Characterization of β-lactamase from Mycobacterium smegmatis SN2
No full textβ -Lactamase fromMycohacterium smegamatis SN2 was purified to homogeneity. The molecular weight of the enzyme was 30,000 and the isoelectric point was 4.1. The enzyme showed maximal activity at pH 6.5 and 56°C and resembled the plasmid-mediated TEM-type β -lactamases commonly encountered in gram-negative bacteria in substrate profile. The enzyme shared antigenic structure with β -lactamase from Mycobacterium butyricum ATCC 19979 and Escherichia coli HB101 (pBR322)
- …
