Klebsiella

Resistant Gram-negative organisms such as Klebsiella pneumoniae and Enterobacter aerogenes. 

AN AMPEROMETRIC ENZYME IMMUNOSENSOR BASED ON SCREEN-PRINTED ELECTRODE FOR THE DETERMINATION OF KLEBSIELLA PNEUMONIAE BACTERIAL ANTIGEN... 

The aim of our investigation was the development of the amperometric enzyme immunosensor for the determination of Klebsiella pneumoniae bacterial antigen (Ag), causes the different inflammatory diseases. The biosensing pail of the sensors consisted of the enzyme (cholinesterase) and antibodies (Ab) immobilized on the working surface of the screen-printed electrode. Bovine seiaim albumin was used as a matrix component. 

It was established that Ab to Klebsiella pneumoniae didn t demonstrate the cross-reactivity to antigens of the relative bacterial species so, it could be considered that antibodies investigated was highly specific only to the own antigen. The physical-chemical characteristics of the immunological interaction such as constants of formation of Ag-Ab complex were obtained. The binding constants of immune complex were Ka =(9.7 l.l)-10 and Ka,=(1.7+0.3)T0 (mg/ml)f... 

The developed amperometric enzyme immunosensor was probed to determine the Klebsiella pneumoniae antigen in the human sera samples. The obtained results were juxtaposed with the data of the bacteriological analysis. 

I Citrobacter freundii Klebsiella pneumoniae Enterobacter cloacae Yersinia enterocolitica... 

Figure 17.14 Model of evolved mutant from cephalosphorinase shuffling. The sequence of the most active cephalosporinase mutant was modeled using the crystal structure of the class C cephalosporinase from Enterobacter cloacae. The mutant and wild-type proteins were 63% identical. This chimeric protein contained portions from three of the starting genes, including Enterobacter (blue), Klebsiella (yellow), and Citrobacter (green), as well as 33 point mutations (red). (Courtesy of A. Crameri.)...

Gentamidns C, Ci and Ci. Acylation 3-/V-Acetyl derivatives of the respective substrates Escherichia coli Klebsiella penumoniae Pseudomonas aeruginosa... 

Kanamydn A Kanamycin B Escherichia coli Klebsiella pneumoniae Pseudomonas aeruginosa... 

The sulfonamides are often used to control urinary tract infections caused by certain bacteria such as Escherichia coli, Staphylococcus aureus, and Klebsiella-Enterobacter. Mafenide (Sulfamylon) and silver sulfadiazine (Silvadene) are topical sulfonamides used in the treatment of second- and third-degree bums. Additional uses of the sulfonamides are given in the Summary Drug Table The Sulfonamides. 

Meropenem (Merrem IV) inhibits syndiesis of die bacterial cell wall and causes die deadi of susceptible cells. This drug is used for intra-abdominal infections caused by Pseudomonas aeruginosa, Escherichia coli, Klebsiella pneumoniae, and odier susceptible organisms Meropenem also is effective against bacterial meningitis caused by Neisseria meningitidis, Streptococcus pneumoniae, and Hemophilus influenzae. 

Among other polysaccharides studied were those elaborated by Neisseria per-flava (starch-type polysaccharide), Polytomella coeca (a starch richer in amy-lopectin than most natural starches), Pseudomonas morsprunorum (Wormald) (levan), Acetobacter acetigenum (cellulose), Aerobacter aerogenes (NCTC 8172) (Klebsiella Type 164), Bacillus megaterium. Bacterium pruni, and Bacterium prunicola (polyfructoses of the levan type). 

The hydrolysis with a (R)-specific amidase from Klebsiella oxytoca resolved 2-hydroxy- and 2-amino-3,3,3-trifluoro-2-methylpropionamide, giving the (R)-acid and the remaining (S)-amide (Figure 6.39) [104,105]. 

The nitrogenase proteins are generally characterized by two letters indicating the species and strains of bacteria and the numerals 1 for the MoFe protein and 2 for the Fe protein. Thus, the Fe protein from Azotobacter vinelandii is Av2 and the MoFe protein from Klebsiella pneumoniae is Kpl. 

Figure 3 shows the three-dimensional structure of the MoFe protein from Klebsiella pneumoniae, Kpl, obtained at 1.65-A resolution (7). The overall structure of the polypeptides is frilly consistent with that reported earlier for Avl (3). The a and /8 subunits exhibit similar polypeptide folds with three domains of parallel /3 sheet/a helical type. At the interface between the three domains in the a subunit is a wide shallow cleft with the FeMoco at the bottom of the cleft about 10 A from the solvent. FeMoco is enclosed within the a subunit. The P cluster, however, is buried within the protein at the interface between the a and /8 subunits, being bound by cysteine residues from each subunit. A pseudo-twofold rotation axis passes between the two halves of the P cluster and relates the a and (3 subunits. Each af3 pair of subunits contains one FeMoco and one P cluster and thus appears... 

Fig. 3. The tetrameric structure of the MoFe protein (Kpl) from Klebsiella pneumoniae (7). The two FeMoco clusters and the P clusters are depicted by space-filling models and the polypeptides by ribbons diagrams (MOLSCRIPT (196)). The FeMoco clusters are bound only to the a subunits, whereas the P clusters span the interface of the a and j8 subunits.

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