Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii
نویسندگان
چکیده
منابع مشابه
Genetic Characterization of Atypical Citrobacter freundii
The ability of a bacterial population to survive in different niches, as well as in stressful and rapidly changing environmental conditions, depends greatly on its genetic content. To survive such fluctuating conditions, bacteria have evolved different mechanisms to modulate phenotypic variations and related strategies to produce high levels of genetic diversity. Laboratories working in microbi...
متن کاملIsolation and Characterization of Cytotoxic, Aggregative Citrobacter freundii
Citrobacter freundii is an infrequent but established cause of diarrhea in humans. However, little is known of its genetic diversity and potential for virulence. We analyzed 26 isolates, including 12 from human diarrheal patients, 2 from human fecal samples of unknown diarrheal status, and 12 from animals, insects, and other sources. Pulsed field gel electrophoresis using XbaI allowed us to div...
متن کاملPurification and Characterization of Alginate Lyase from Mucoid Pseudomonas aeruginosa Strain 214
Pseudomonas aeruginosa is an opportunistic pathogen that causes a variety of infections in compromised patients. The ability of Pseudomonas aeruginosa to produce chronic infection is based in part on its ability to biosynthesis of biofilm, and alginate is the major polysaccharide in the synthesized biofilm. So alginate degradation is very essential in the dispersion of Pseudomonas aeruginosa bi...
متن کاملA new restriction endonuclease from Citrobacter freundii.
CfrI, a new restriction endonuclease of unique substrate specificity, has been isolated from a Citrobacterfreundii strain. The enzyme recognizes a degenerated sequence PyGGCCPu in double-strand DNA and cleaves it between Py and G residues to yield 5' -protruding tetranucleotide ends GGCC.
متن کاملInteraction of cefpirome and a cephalosporinase from Citrobacter freundii GN7391.
The interaction of cefpirome and a cephalosporinase from Citrobacter freundii, including hydrolysis and inhibition, was studied in comparison with those of cefotiam, cefotaxime, and ceftazidime. Cefpirome was hydrolyzed by the enzyme more rapidly at Vmax than were cefotaxime and ceftazidime. However, the low affinity of the enzyme for cefpirome caused a reduction in the hydrolytic rate of cefpi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1985
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.163.2.669-676.1985