Results 311 to 320 of about 637,867 (346)
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Microbiologica, 1986
Penicillin-binding protein 5 of Streptococcus faecium has been solubilized and partially separated from other membrane proteins by covalent affinity chromatography. PBP 5 was successively purified to homogeneity by resolution on SDS-polyacrylamide gel, elution and renaturation of penicillin-binding activity.
A. Grossato +4 more
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Penicillin-binding protein 5 of Streptococcus faecium has been solubilized and partially separated from other membrane proteins by covalent affinity chromatography. PBP 5 was successively purified to homogeneity by resolution on SDS-polyacrylamide gel, elution and renaturation of penicillin-binding activity.
A. Grossato +4 more
openaire +2 more sources
Penicillin-Binding Proteins inFusobacteriumSpecies
Anaerobe, 1996Abstract PBPs were identified in four species ofFusobacterium. Each species had a distinctive PBP pattern, although some intra-species variation was noted. Most species had five or six PBPs, ranging in molecular weight from ∼100 kDa to ∼40 kDa. The two strains ofF. nucleatumtested had characteristic “wavy” PBP patterns.F. mortiferumwas distinctive in
K. Tunér +3 more
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Penicillin-binding proteins of clostridia
Current Microbiology, 1993The penicillin-binding protein (PBP) profiles of 33Clostridium perfringens and sixClostridium species isolated from clinically significant infections were analyzed. Three new PBPs—PBPs 2B, 4B, and 5B (84, 70, and 49 kDa respectively)—and a high-molecular-weight PBP 6 (45 kDa) were demonstrated in theC. perfringens isolates. In addition to PBPs 1 and 2,
Lynda Chalkley +1 more
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The Journal of Biochemistry, 1988
We determined the active site of penicillin-binding protein (PBP) 2 of Escherichia coli. A water-soluble form of PBP 2, which was constructed by site-directed mutagenesis, was purified by affinity chromatography, labeled with dansyl-penicillin, and then digested with a combination of proteases.
A, Takasuga +5 more
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We determined the active site of penicillin-binding protein (PBP) 2 of Escherichia coli. A water-soluble form of PBP 2, which was constructed by site-directed mutagenesis, was purified by affinity chromatography, labeled with dansyl-penicillin, and then digested with a combination of proteases.
A, Takasuga +5 more
openaire +2 more sources
Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to β-lactam agents
International Journal of Antimicrobial Agents, 2010Chiranjit Chowdhury, Anindya S Ghosh
exaly

