BIOMAT Database Logo BIOMAT Database Logo

In vivo activation by polymyxin B of phospholipase C from Pseudomonas aeruginosa. 1977

T Kusano, and K Izaki, and H Takahashi

UI MeSH Term Description Entries
D010740 Phospholipases A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-. Lecithinases,Lecithinase,Phospholipase
D011112 Polymyxin B A mixture of polymyxins B1 and B2, obtained from BACILLUS POLYMYXA strains. They are basic polypeptides of about eight amino acids and have cationic detergent action on cell membranes. Polymyxin B is used for treatment of infections with gram-negative bacteria, but may be neurotoxic and nephrotoxic. Aerosporin,Polymyxin B Sulfate
D011113 Polymyxins Basic lipopeptide antibiotic group obtained from Bacillus polymyxa. They affect the cell membrane by detergent action and may cause neuromuscular and kidney damage. At least eleven different members of the polymyxin group have been identified, each designated by a letter. Polymyxin,Polymyxin M
D011550 Pseudomonas aeruginosa A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection. Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D002701 Chloramphenicol An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106) Cloranfenicol,Kloramfenikol,Levomycetin,Amphenicol,Amphenicols,Chlornitromycin,Chlorocid,Chloromycetin,Detreomycin,Ophthochlor,Syntomycin
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations

Related Publications

T Kusano, and K Izaki, and H Takahashi
In vivo studies with two phospholipase C fractions from Pseudomonas aeruginosa.
July 1987, Infection and immunity,
T Kusano, and K Izaki, and H Takahashi
[Polymyxin B in meningitis Pseudomonas aeruginosa].
November 1960, La Semana medica,
T Kusano, and K Izaki, and H Takahashi
In vivo and in vitro toxicity of phospholipase C from Pseudomonas aeruginosa.
February 1992, Toxicon : official journal of the International Society on Toxinology,
T Kusano, and K Izaki, and H Takahashi
Platelet aggregation by a phospholipase C from Pseudomonas aeruginosa.
September 1988, Thrombosis research,
T Kusano, and K Izaki, and H Takahashi
[Meningitis caused by Pseudomonas aeruginosa, treated by polymyxin B].
February 1955, La Tunisie medicale,
T Kusano, and K Izaki, and H Takahashi
Secretion of phospholipase C by Pseudomonas aeruginosa.
August 1979, Infection and immunity,
T Kusano, and K Izaki, and H Takahashi
Pharmacodynamics of polymyxin B against Pseudomonas aeruginosa.
September 2005, Antimicrobial agents and chemotherapy,
T Kusano, and K Izaki, and H Takahashi
Fatty acid alterations and polymyxin B binding by lipopolysaccharides from Pseudomonas aeruginosa adapted to polymyxin B resistance.
October 1989, Antimicrobial agents and chemotherapy,
T Kusano, and K Izaki, and H Takahashi
Treatment of pseudomonas aeruginosa ulcer with polymyxin B.
October 1952, A.M.A. archives of ophthalmology,
T Kusano, and K Izaki, and H Takahashi
Infections with Pseudomonas aeruginosa treated with polymyxin B.
January 1952, A.M.A. archives of internal medicine,
Copied contents to your clipboard!