Results 221 to 230 of about 400,542 (252)

Identification of the Penicillin-Binding Active Site of Penicillin-Binding Protein 2 of Escherichia coli

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, H, Adachi, F, Ishino, M, Matsuhashi, T, Ohta, H, Matsuzawa   +5 more
openaire   +2 more sources

Penicillin-Binding Proteins inFusobacteriumSpecies

Anaerobe, 1996
Abstract 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, H.M. Wexler, D. Reeves, S.M. Finegold   +3 more
openaire   +1 more source

Penicillin-binding proteins of clostridia

Current Microbiology, 1993
The 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, Ingrid Van der Westhuyzen   +1 more
openaire   +1 more source

Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein.

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, Y. R. Cheng, E. Tonin, P. Jacques, FONTANA, Roberta   +4 more
openaire   +2 more sources

Penicillin-Binding Proteins of Gram-Negative Bacteria

Clinical Infectious Diseases, 1988
beta-Lactam antibiotics exert their antibacterial effects by inactivating the high-molecular-weight penicillin-binding proteins (PBPs) that are responsible for the final stages of peptidoglycan biosynthesis. The availability of the amino acid sequences of several low-molecular-weight PBPs, high-molecular-weight PBPs, and active-site serine beta ...
B G, Spratt, K D, Cromie
openaire   +2 more sources

Analysis of Amino Acid Sequences of Penicillin-Binding Proteins 1a, 2b, and 2x in Invasive Streptococcus pneumoniae Nonsusceptible to Penicillin Isolated from Children in India

Microbial Drug Resistance, 2021
Balaji Veeraraghavan, Rosemol Varghese, Ayyanraj Neeravi   +2 more
exaly  

Relationship between Penicillin-Binding Proteins Alterations and β-Lactams Non-Susceptibility of Diseased Pig-Isolated Streptococcus suis

Antibiotics, 2023
Suganya Yongkiettrakul, Pornchalit Assavacheep, Kamonwan Lunha   +2 more
exaly  

Expanded profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39

Biological Chemistry, 2022
Erin Carlson, Deepti Sharan
exaly  

PENICILLIN-BINDING PROTEIN INHIBITORS

2018
BURNS CHRISTOPHER J, DAIGLE DENIS, CHU GUO-HUA, HAMRICK JODIE, LUCAS MATTHEW, BOYD STEVEN A, ZULLI ALLISON L, MESAROS EUGEN F, CONDON STEPHEN M, TROUT ROBERT E LEE, MYERS CULLEN L   +10 more
openaire   +10 more sources

Penicillin-binding Protein

2006
openaire   +2 more sources